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Information on EC 2.3.2.8 - arginyltransferase
for references in articles please use BRENDA:EC2.3.2.8
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IUBMB Comments
Requires 2-sulfanylethan-1-ol (2-mercaptoethanol) and a univalent cation. Peptides and proteins containing an N-terminal glutamate, aspartate or cystine residue can act as acceptors.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 2.3.2.8
-
arginylation
-
2.5.1.18
-
rx:glutathione
- rx
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n-degrons
-
polyubiquitylates
- medicine
- agriculture
showSynonyms
arginyltransferase, r-transferase, arginyl-trna-protein transferase, arginyl-trna protein transferase, arg-transferase, arginyltransferase 1, arginyl transferase, arginyl-transferase, arginyl-trna:protein arginyltransferase, ate1-1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Arg-transferase
Arg-tRNA-protein transferase
arginyl tRNA transferase
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-
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arginyl-transfer ribonucleate-protein aminoacyltransferase
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arginyl-transfer ribonucleate-protein transferase
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arginyl-transferase
arginyl-tRNA protein transferase
arginyl-tRNA--protein transferase
arginyl-tRNA-protein transferase
arginyltransferase
arginyltransferase 1
arginyltransferase ATE1
ATE
Ate1
Ate1-3
Ate1-4
DdAte1
L-arginyltransferase
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R-transferase
arginyl-tRNA protein transferase
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Ate1
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R-transferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-arginyl-tRNAArg + protein = tRNAArg + L-arginyl-[protein]
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
arginylation
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
MetaCyc
Arg/N-end rule pathway (eukaryotic)
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SYSTEMATIC NAME
IUBMB Comments
L-arginyl-tRNAArg:protein arginyltransferase
Requires 2-sulfanylethan-1-ol (2-mercaptoethanol) and a univalent cation. Peptides and proteins containing an N-terminal glutamate, aspartate or cystine residue can act as acceptors.
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CAS REGISTRY NUMBER
COMMENTARY
37257-24-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Arg-tRNA + apolipoprotein A-I
tRNAArg + L-Arg-[apolipoprotein A-I]
-
Substrates: -
Products: -
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L-Arg-tRNAArg + alpha-1-antitrypsin
tRNAArg + L-Arg-[alpha-1-antitrypsin]
-
Substrates: -
Products: -
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L-Arg-tRNAArg + apolipoprotein E
tRNAArg + L-Arg-[apolipoprotein E]
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Substrates: -
Products: -
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L-Arg-tRNAArg + calreticulin
tRNAArg + L-Arg-[calreticulin]
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Substrates: -
Products: -
Products: -
?
L-Arg-tRNAArg + contrapsin-like protease inhibitor-3
tRNAArg + L-Arg-[contrapsin-like protease inhibitor-3]
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Substrates: -
Products: -
Products: -
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L-Arg-tRNAArg + Cys-beta-galactosidase
tRNaArg + L-Arg-L-Cys-beta-galactosidase
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Substrates: substrate only for isoforms Ate1-3, Ate1-4
Products: -
Products: -
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L-Arg-tRNAArg + glucose-related protein 78
tRNAArg + L-Arg-[glucose-related protein 78]
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Substrates: -
Products: -
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L-Arg-tRNAArg + hemopexin
tRNAArg + L-Arg-[hemopexin]
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Substrates: -
Products: -
Products: -
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L-Arg-tRNAArg + protein-disulfide isomerase
tRNAArg + L-Arg-[protein-disulfide isomerase]
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Substrates: -
Products: -
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?
L-arginyl-tRNA + L-Asp-beta-galactosidase
tRNA + L-arginyl-L-Asp-beta-galactosidase
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + alpha cardiac actin
tRNAArg + L-arginyl-[alpha cardiac actin]
Substrates: -
Products: -
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L-arginyl-tRNAArg + alpha-synuclein
tRNAArg + L-arginyl-[alpha-synuclein]
Substrates: alpha-syn is arginylated in vitro and in vivo
Products: -
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L-arginyl-tRNAArg + Asp-beta-galactosidase
tRNAArg + L-arginyl-Asp-beta-galactosidase
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + BiP/GRP78 protein
tRNAArg + L-arginyl-[BiP/GRP78 protein]
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Substrates: -
Products: -
Products: -
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L-arginyl-tRNAArg + bovine alpha-lactalbumin
tRNAArg + L-arginyl-[bovine alpha-lactalbumin]
-
Substrates: higher activity is detected with isoforms ATE1-1 (100%) and ATE1-2 (85%), and weaker activity is detected with isoforms ATE1-3 (18%) and ATE1-4 (4%)
Products: -
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L-arginyl-tRNAArg + calreticulin
tRNAArg + L-arginyl-[calreticulin]
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Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + EBP
tRNAArg + L-arginyl-[EBP]
Substrates: Pseudomonas syringae ethylene response factor 72 (EBP) is a putative substrate for ATE1
Products: -
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L-arginyl-tRNAArg + fructose diphosphatase
tRNAArg + L-Arg-[fructose diphosphatase]
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Substrates: from rabbit liver
Products: -
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L-arginyl-tRNAArg + immunoglobulin
tRNAArg + L-arginyl-[immunoglobulin]
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Substrates: kappa-light chain of immunoglobulin
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L-arginyl-tRNAArg + L-Arg-[beta-galactosidase]
tRNAArg + L-Arg-L-Arg-[beta-galactosidase]
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Substrates: -
Products: -
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L-arginyl-tRNAArg + L-Asp-L-Ala
tRNAArg + L-Arg-L-Asp-L-Ala
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Substrates: other dipeptides: overview
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L-arginyl-tRNAArg + L-aspartic acid
tRNAArg + L-Arg-L-Asp
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Substrates: poor substrate
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L-arginyl-tRNAArg + L-cystinyl-bis-L-Ala
tRNAArg + L-Arg-L-cystinyl-bis-L-Ala
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Substrates: poor substrate
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L-arginyl-tRNAArg + L-Glu-L-Ala
tRNAArg + L-Arg-L-Glu-L-Ala
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Substrates: other dipeptides: overview, not dipeptides with D-Glu
Products: -
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L-arginyl-tRNAArg + L-Glu-L-Ala-L-Ala
tRNAArg + L-Arg-L-Glu-L-Ala-L-Ala
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Substrates: other tripeptides: overview
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L-arginyl-tRNAArg + L-Glu-[beta-galactosidase]
tRNAArg + L-Arg-L-Glu-[beta-galactosidase]
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Substrates: -
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L-arginyl-tRNAArg + L-glutamic acid
tRNAArg + L-Arg-L-Glu
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Substrates: poor substrate
Products: -
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L-arginyl-tRNAArg + L-isoasparagine
tRNAArg + L-arginyl-L-isoasparagine
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Substrates: non-peptide-derivatives of dicarboxylic amino acids with blocked alpha-carboxyl group and unsubstituted beta- or gamma-carboxyl group, such as isoasparagine and isoglutamine
Products: -
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L-arginyl-tRNAArg + L-isoglutamine
tRNAArg + L-arginyl-L-isoglutamine
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Substrates: non-peptide-derivatives of dicarboxylic amino acids with blocked alpha-carboxyl group and unsubstituted beta- or gamma-carboxyl group, such as isoasparagine and isoglutamine
Products: -
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L-arginyl-tRNAArg + L-Met-[beta-galactosidase]
tRNAArg + L-Arg-L-Met-[beta-galactosidase]
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Substrates: -
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L-arginyl-tRNAArg + N-L-aspartyl-N'-dansylamido-1,4-butanediamine
tRNAArg + N-(L-arginyl-L-aspartyl)-N'-dansylamido-1,4-butanediamine
L-arginyl-tRNAArg + protein disulfide isomerase
tRNAArg + L-arginyl-[protein disulfide isomerase]
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Substrates: -
Products: -
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L-arginyl-tRNAArg + Rgs16 regulator of G protein
tRNAArg + L-arginyl-[Rgs16 regulator of G protein]
Substrates: -
Products: -
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L-arginyl-tRNAArg + Rgs4 regulator of G protein
tRNAArg + L-arginyl-[Rgs4 regulator of G protein]
Substrates: -
Products: -
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L-arginyl-tRNAArg + Rgs5 regulator of G protein
tRNAArg + L-arginyl-[Rgs5 regulator of G protein]
Substrates: -
Products: -
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L-arginyl-tRNAArg + RIN4
tRNAArg + L-arginyl-[RIN4]
Substrates: Pseudomonas syringae 1-interacting protein 4 (RIN4) is a putative substrate for ATE1
Products: -
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L-arginyl-tRNAArg + transaldolase
tRNAArg + L-arginyl-[transaldolase]
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Substrates: I and III from Candida
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L-arginyl-tRNAArg + trypsin inhibitor
tRNAArg + L-arginyl-[trypsin inhibitor]
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Substrates: from soybean
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L-arginyl-tRNAArg + VRN2
tRNAArg + L-arginyl-[VRN2]
Substrates: Pseudomonas syringae vernalization 2 protein (VRN2) is a putative substrate for ATE1
Products: -
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L-arginyl-tRNAAsp + beta-actin
tRNAAsp + L-arginyl-[beta-actin]
-
Substrates: -
Products: -
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?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
Substrates: -
Products: -
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
Products: -
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
Substrates: ATE1-2p is less active than ATE1-1p
Products: -
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
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Substrates: addition to amino-terminus
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
Substrates: -
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
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Substrates: involved in ubiquitin mediated protein degradation
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
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Substrates: addition to amino-terminus
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
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Substrates: acceptor proteins require an acidic amino terminus, an Asp- or Glu-residue at the acceptor site
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
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Substrates: addition to amino-terminus
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
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Substrates: possibly involved in degradation of proteins with acidic NH2-termini
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
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Substrates: catalyzes post-translational ribosome-independent modification of certain acceptor proteins
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?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
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L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
Products: -
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?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: involved in ubiquitin mediated protein degradation
Products: -
Products: -
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + albumin
tRNAArg + L-arginyl-albumin
-
Substrates: from bovine serum
Products: -
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L-arginyl-tRNAArg + albumin
tRNAArg + L-arginyl-albumin
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Substrates: from bovine serum, accepts 1 mol arginine/mol
Products: -
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?
L-arginyl-tRNAArg + alpha lactalbumin
tRNAArg + L-arginyl-[lactalbumin]
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Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + alpha lactalbumin
tRNAArg + L-arginyl-[lactalbumin]
-
Substrates: bovine
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L-arginyl-tRNAArg + alpha lactalbumin
tRNAArg + L-arginyl-[lactalbumin]
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Substrates: -
Products: -
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?
L-arginyl-tRNAArg + beta-actin
tRNAArg + L-arginyl-[beta-actin]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + beta-actin
tRNAArg + L-arginyl-[beta-actin]
Substrates: -
Products: -
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?
L-arginyl-tRNAArg + beta-actin
tRNAArg + L-arginyl-[beta-actin]
Substrates: -
Products: -
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L-arginyl-tRNAArg + bovine serum albumin
tRNAArg + L-arginyl-[bovine serum albumin]
-
Substrates: -
Products: -
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L-arginyl-tRNAArg + bovine serum albumin
tRNAArg + L-arginyl-[bovine serum albumin]
-
Substrates: high activity is detected with isoforms ATE1-1 (100%) and ATE1-2 (95%), and weaker activity is detected with isoforms ATE1-3 (10%) and ATE1-4 (4%)
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L-arginyl-tRNAArg + ERF-VII peptide
tRNAArg + L-arginyl-[ERF-VII peptide]
Substrates: after N-terminal Cys-sulfinic acid formation on ERF-VII peptide through plant cysteine oxidase. An ERF-VII peptide with an N-terminal Gly does not accept Arg, whereas an N-terminal Asp accepts Arg, independent of the presence of PCO1 or 4. A peptide comprising an N-terminal Cys-sulfonic acid is also shown to be a substrate for ATE1, again independent of the presence of PCO1 or 4. Proposed arginylation requirements for the Arg/Cys branch of the N-end rule pathway
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L-arginyl-tRNAArg + ERF-VII peptide
tRNAArg + L-arginyl-[ERF-VII peptide]
Substrates: after N-terminal Cys-sulfinic acid formation on ERF-VII peeptide through plant cysteine oxidase. C-terminally biotinylated RAP22-13 peptides (H2N-XGGAIISDFIPP(PEG)K(biotin)-NH2) where the N-terminal residue, X, constitutes Gly, Asp, Cys or Cys-sulfonic acid are subjected to the arginylation assay in the presence or absence of PCO1/4. An ERF-VII peptide with an N-terminal Gly does not accept Arg, whereas an N-terminal Asp accepts Arg, independent of the presence of PCO1 or 4. A peptide comprising an N-terminal Cys-sulfonic acid is also shown to be a substrate for ATE1, again independent of the presence of PCO1 or 4. Arginylation of the 12-mer peptide substrates, peptide sequences, overview
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L-arginyl-tRNAArg + insulin
tRNAArg + L-arginyl-[insulin]
-
Substrates: -
Products: -
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L-arginyl-tRNAArg + insulin
tRNAArg + L-arginyl-[insulin]
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Substrates: less effective
Products: -
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L-arginyl-tRNAArg + N-L-aspartyl-N'-dansylamido-1,4-butanediamine
tRNAArg + N-(L-arginyl-L-aspartyl)-N'-dansylamido-1,4-butanediamine
-
Substrates: -
Products: -
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L-arginyl-tRNAArg + N-L-aspartyl-N'-dansylamido-1,4-butanediamine
tRNAArg + N-(L-arginyl-L-aspartyl)-N'-dansylamido-1,4-butanediamine
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Substrates: i.e. Asp(4)DNS
Products: i.e. ArgAsp(4)DNS
Products: i.e. ArgAsp(4)DNS
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: the enzyme transfers the amino acid arginine from Arg-tRNAArg to the N-terminal residues of proteins, such as aspartate, glutamate, and oxidized cysteine. The resulting N-terminal-Arg acts as an N-degron that regulates the degradation of various biomaterials via the ubiquitin/Ub-proteasome system (UPS) or the autophagy-lysosome system (ALS). Arginyltransferase 1 achieves the selectivity for its peptidyl-ligands through these multivalent interactions, with Kd values in the micro-molar range
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: human ATE1 includes a unique and extended loop that wraps around tRNAArg, creating extensive contacts with the T-arm of the tRNA cofactor
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: structural analysis of human ATE1 isoforms and their interactions with Arg-tRNAArg
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
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Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
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Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
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Substrates: the enzyme catalyzes mid-chain arginylation of proteins at side chain carboxylates in vivo. N-terminal arginylation of the peptide substrates occurs by the alpha amino group
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: presence of an intrinsically disordered region (IDR) that is conserved in most arginyltransferases 1 (ATE1s). This IDR may play a regulatory role in post-translational arginylation. The IDR may be involved in enhancing the affinity of ATE1 for Arg-tRNAArg
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Mus musculus 129SvEv/C57BL/6
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
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L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
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L-arginyl-tRNAArg + RGS4 protein
tRNAArg + L-arginyl-[RGS4 protein]
Substrates: -
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L-arginyl-tRNAArg + RGS4 protein
tRNAArg + L-arginyl-[RGS4 protein]
Mus musculus 129SvEv/C57BL/6
Substrates: -
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L-arginyl-tRNAArg + thyroglobulin
tRNAArg + L-arginyl-[thyroglobulin]
-
Substrates: -
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L-arginyl-tRNAArg + thyroglobulin
tRNAArg + L-arginyl-[thyroglobulin]
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Substrates: accepts 2 mol arginine/mol
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additional information
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Substrates: putative substrates of ATE are identified among Nt Met-Cys proteins. N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
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additional information
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Substrates: N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
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additional information
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Substrates: identification of four arginylation sites in the most abundant actin isoform of Dictyostelium discoideum, in addition to arginylation sites in other actin isoforms and several actin-binding proteins
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additional information
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Substrates: identification of four arginylation sites in the most abundant actin isoform of Dictyostelium discoideum, in addition to arginylation sites in other actin isoforms and several actin-binding proteins
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additional information
?
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Substrates: identification of four arginylation sites in the most abundant actin isoform of Dictyostelium discoideum, in addition to arginylation sites in other actin isoforms and several actin-binding proteins
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additional information
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Substrates: the Arg/N-end rule-mediated autophagic flux regulator might be a direct substrate of ATE1, rather than UBR1 or UBR2
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?
additional information
?
-
Substrates: usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts
Products: -
Products: -
?
additional information
?
-
-
Substrates: usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoforms Ate1-3, Ate1-4, no substrate: proteins containing N-terminal Asp or Glu
Products: -
Products: -
?
additional information
?
-
-
Substrates: the arginylation reaction does not require the formation of an ATE1-arginyl-tRNA synthetase complex or the presence of ATP
Products: -
Products: -
?
additional information
?
-
-
Substrates: ATE1 is capable of self-arginylation in vitro and in vivo
Products: -
Products: -
?
additional information
?
-
-
Substrates: Liat1 protein binds to the mouse Ate1 enzyme, but is apparently not arginylated by it
Products: -
Products: -
?
additional information
?
-
Substrates: the Arg/N-end rule-mediated autophagic flux regulator might be a direct substrate of ATE1, rather than UBR1 or UBR2
Products: -
Products: -
?
additional information
?
-
Substrates: usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts
Products: -
Products: -
?
additional information
?
-
-
Substrates: usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts
Products: -
Products: -
?
additional information
?
-
Substrates: the four mouse ATE1 isoforms have different, partially overlapping substrate specificity toward their N-terminal target sites, detailed overview. The four mouse ATE1 isoforms show prominent and consistent differences in target site specificity, both at the N-terminus and the side chain sites. At the N-terminal sites, only three of the four ATE1 isoforms (ATE1-1, 2, and 3) show high preference for the peptides containing N-terminal D and E. ATE1-4 do not appear to target peptides containing N-terminal E. At the same time all four isoforms, to a various degree, show prominent reactivity with the peptides bearing N-terminal C. Even more strikingly, ATE1-1, unlike any other ATE1 isoforms, appears to be reactive with additional N-terminal sites not seen with other ATE1 isoforms, including Q and, weakly, H. Thus, it appears that N-terminal target site specificity of ATE1-1 may be broader than other ATE1 isoforms and potentially include non-canonical N-terminal residues. The four ATE1 isoforms also show different reactivity with the peptides bearing side chain target sites. In the case of ATE1-1 and ATE1-2, the signal with these peptides containing side chain target sites is substantially lower or absent compared to the peptides containing favorable N-terminal target sites. Side chain arginylation of one of these peptides with ATE1-2 in solution. It appears likely that the peptide array format is unfavorable for side chain targeting by these ATE1 isoforms. Isozyme ATE1-1 catalyzes arginylation of non-canonical residues. Identification of the arginylation-favorable sequence motif
Products: -
Products: -
?
additional information
?
-
-
Substrates: the four mouse ATE1 isoforms have different, partially overlapping substrate specificity toward their N-terminal target sites, detailed overview. The four mouse ATE1 isoforms show prominent and consistent differences in target site specificity, both at the N-terminus and the side chain sites. At the N-terminal sites, only three of the four ATE1 isoforms (ATE1-1, 2, and 3) show high preference for the peptides containing N-terminal D and E. ATE1-4 do not appear to target peptides containing N-terminal E. At the same time all four isoforms, to a various degree, show prominent reactivity with the peptides bearing N-terminal C. Even more strikingly, ATE1-1, unlike any other ATE1 isoforms, appears to be reactive with additional N-terminal sites not seen with other ATE1 isoforms, including Q and, weakly, H. Thus, it appears that N-terminal target site specificity of ATE1-1 may be broader than other ATE1 isoforms and potentially include non-canonical N-terminal residues. The four ATE1 isoforms also show different reactivity with the peptides bearing side chain target sites. In the case of ATE1-1 and ATE1-2, the signal with these peptides containing side chain target sites is substantially lower or absent compared to the peptides containing favorable N-terminal target sites. Side chain arginylation of one of these peptides with ATE1-2 in solution. It appears likely that the peptide array format is unfavorable for side chain targeting by these ATE1 isoforms. Isozyme ATE1-1 catalyzes arginylation of non-canonical residues. Identification of the arginylation-favorable sequence motif
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Products: -
?
additional information
?
-
Substrates: N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
Products: -
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?
additional information
?
-
Substrates: the enzyme interacts with sHSP17.2a, an Hsp20 class I chaperone
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme interacts with sHSP17.2a, an Hsp20 class I chaperone
Products: -
Products: -
?
additional information
?
-
Substrates: N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
Products: -
Products: -
?
additional information
?
-
Substrates: N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrates may reach the cytosol by retro-translocation from the endoplasmic reticulum and then be arginylated
Products: -
Products: -
?
additional information
?
-
-
Substrates: interaction of enzyme and N-terminal domain of topoisomerase II. Role in Ate1 in modulating the level of topoisomerase through the cell cycle
Products: -
Products: -
?
additional information
?
-
-
Substrates: usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts
Products: -
Products: -
?
additional information
?
-
-
Substrates: usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts
Products: -
Products: -
?
additional information
?
-
Substrates: N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
Products: -
Products: -
?
additional information
?
-
Substrates: N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Arg-tRNA + apolipoprotein A-I
tRNAArg + L-Arg-[apolipoprotein A-I]
-
Substrates: -
Products: -
Products: -
?
L-Arg-tRNAArg + alpha-1-antitrypsin
tRNAArg + L-Arg-[alpha-1-antitrypsin]
-
Substrates: -
Products: -
Products: -
?
L-Arg-tRNAArg + apolipoprotein E
tRNAArg + L-Arg-[apolipoprotein E]
-
Substrates: -
Products: -
Products: -
?
L-Arg-tRNAArg + calreticulin
tRNAArg + L-Arg-[calreticulin]
-
Substrates: -
Products: -
Products: -
?
L-Arg-tRNAArg + contrapsin-like protease inhibitor-3
tRNAArg + L-Arg-[contrapsin-like protease inhibitor-3]
-
Substrates: -
Products: -
Products: -
?
L-Arg-tRNAArg + glucose-related protein 78
tRNAArg + L-Arg-[glucose-related protein 78]
-
Substrates: -
Products: -
Products: -
?
L-Arg-tRNAArg + hemopexin
tRNAArg + L-Arg-[hemopexin]
-
Substrates: -
Products: -
Products: -
?
L-Arg-tRNAArg + protein-disulfide isomerase
tRNAArg + L-Arg-[protein-disulfide isomerase]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + alpha-synuclein
tRNAArg + L-arginyl-[alpha-synuclein]
Substrates: alpha-syn is arginylated in vitro and in vivo
Products: -
Products: -
?
L-arginyl-tRNAArg + beta-actin
tRNAArg + L-arginyl-[beta-actin]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + BiP/GRP78 protein
tRNAArg + L-arginyl-[BiP/GRP78 protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + calreticulin
tRNAArg + L-arginyl-[calreticulin]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + ERF-VII peptide
tRNAArg + L-arginyl-[ERF-VII peptide]
Substrates: after N-terminal Cys-sulfinic acid formation on ERF-VII peptide through plant cysteine oxidase. An ERF-VII peptide with an N-terminal Gly does not accept Arg, whereas an N-terminal Asp accepts Arg, independent of the presence of PCO1 or 4. A peptide comprising an N-terminal Cys-sulfonic acid is also shown to be a substrate for ATE1, again independent of the presence of PCO1 or 4. Proposed arginylation requirements for the Arg/Cys branch of the N-end rule pathway
Products: -
Products: -
?
L-arginyl-tRNAArg + protein disulfide isomerase
tRNAArg + L-arginyl-[protein disulfide isomerase]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: involved in ubiquitin mediated protein degradation
Products: -
Products: -
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: possibly involved in degradation of proteins with acidic NH2-termini
Products: -
Products: -
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: catalyzes post-translational ribosome-independent modification of certain acceptor proteins
Products: -
Products: -
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: involved in ubiquitin mediated protein degradation
Products: -
Products: -
?
L-arginyl-tRNAArg + acceptor protein
tRNAArg + L-arginyl-[acceptor protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: the enzyme transfers the amino acid arginine from Arg-tRNAArg to the N-terminal residues of proteins, such as aspartate, glutamate, and oxidized cysteine. The resulting N-terminal-Arg acts as an N-degron that regulates the degradation of various biomaterials via the ubiquitin/Ub-proteasome system (UPS) or the autophagy-lysosome system (ALS). Arginyltransferase 1 achieves the selectivity for its peptidyl-ligands through these multivalent interactions, with Kd values in the micro-molar range
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: the enzyme catalyzes mid-chain arginylation of proteins at side chain carboxylates in vivo. N-terminal arginylation of the peptide substrates occurs by the alpha amino group
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Mus musculus 129SvEv/C57BL/6
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + RGS4 protein
tRNAArg + L-arginyl-[RGS4 protein]
Substrates: -
Products: -
Products: -
?
L-arginyl-tRNAArg + RGS4 protein
tRNAArg + L-arginyl-[RGS4 protein]
Mus musculus 129SvEv/C57BL/6
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the Arg/N-end rule-mediated autophagic flux regulator might be a direct substrate of ATE1, rather than UBR1 or UBR2
Products: -
Products: -
?
additional information
?
-
Substrates: the Arg/N-end rule-mediated autophagic flux regulator might be a direct substrate of ATE1, rather than UBR1 or UBR2
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrates may reach the cytosol by retro-translocation from the endoplasmic reticulum and then be arginylated
Products: -
Products: -
?
additional information
?
-
-
Substrates: interaction of enzyme and N-terminal domain of topoisomerase II. Role in Ate1 in modulating the level of topoisomerase through the cell cycle
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S center
-
ATE1 binds an iron-sulfur ([Fe-S]) cluster that appears to function as an oxygen sensor to regulate ATE1 activity. As this cofactor is oxygen-sensitive, purification of ATE1 in the presence of O2 results in cluster decomposition and loss. Anoxic chemical reconstitution to assemble the [Fe-S] cluster cofactor
Fe-S center
ATE1 binds an iron-sulfur ([Fe-S]) cluster that appears to function as an oxygen sensor to regulate ATE1 activity. As this cofactor is oxygen-sensitive, purification of ATE1 in the presence of O2 results in cluster decomposition and loss. Anoxic chemical reconstitution to assemble the [Fe-S] cluster cofactor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
homocysteine-responsive endoplasmic reticlulum protein
i.e. HERP, a key inhibitor of the turnover and N-terminal arginylation of molecular chaperone BiP. HERP is a 43-kDa endoplasmic reticlulum (ER) membrane-integrated protein that is an essential component of ER-associated protein degradation
-
p-[(bromoacetyl)amino]phenylarsenoxide
-
irreversible, potent inhibitor
phenylarsenoxide
-
inhibition below 0.005 mM is fully reversed by excess dithiothreitol
Di- and tripeptides
-
with glutamyl-, asparagyl- and to a lesser extent cystinyl-NH2-terminal residues, competitive to bovine serum albumin acceptor
Di- and tripeptides
-
most potent inhibitor is Glu-Val-Phe, inhibits transfer of arginine to acceptor proteins
hemin
-
Fe3+-heme, inhibits arginyl-transferase through a redox mechanism that involves the formation of disulfide between the enzymes Cys-71 and Cys-72 residues
hemin
-
Fe3+-heme, inhibits arginyl-transferase through a redox mechanism that involves the formation of disulfide between the enzymes Cys-71 and Cys-72 residues
heparin
-
50% inhibition at 0.05 mg/ml, kinetics, competitive to L-arginyl-tRNA
heparin
-
50% inhibition at 0.05 mg/ml, kinetics, competitive to L-arginyl-tRNA
additional information
para-chloroamphetamine, PCA, a specific inhibitor of the arginylation branch of the pathway (Arg/N-end rule pathway). PCA significantly alters various biological pathways, including cellular responses to stress, nutrient, and DNA damage, which are also closely involved in modulation of autophagic responses. Treatment with para-chloroamphetamine (PCA) delays the fusion of autophagosomes with lysosomes and leads to the accumulation of autophagic markers. Analysis of PCA effects in wild-type and mutant (ubr1-/- ubr2-/-) HeLa cells. The direct targets of PCA are UBR1 and UBR2 proteins, not ATE1, an upstream component of the Arg/N-end rule pathway
-
additional information
para-chloroamphetamine, PCA, a specific inhibitor of the arginylation branch of the pathway (Arg/N-end rule pathway). PCA significantly alters various biological pathways, including cellular responses to stress, nutrient, and DNA damage, which are also closely involved in modulation of autophagic responses. Treatment with para-chloroamphetamine (PCA) delays the fusion of autophagosomes with lysosomes and leads to the accumulation of autophagic markers. Analysis of PCA effects in wild-type and mutant (ubr1-/- ubr2-/-) MEFs. The direct targets of PCA are UBR1 and UBR2 proteins, not ATE1, an upstream component of the Arg/N-end rule pathway
-
additional information
-
no inhibition by chondroitinsulfate A, B or C, hyaluronic acid, D-glucosamine N-sulfate, D-glucose 6-sulfate, D-glucosamine, D-galactosamine, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, D-xylose, D-glucuronic acid
-
additional information
-
no inhibition by chondroitinsulfate A, B or C, hyaluronic acid, D-glucosamine N-sulfate, D-glucose 6-sulfate, D-glucosamine, D-galactosamine, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, D-xylose, D-glucuronic acid
-
additional information
-
no inhibition by chondroitinsulfate A, B or C, hyaluronic acid, D-glucosamine N-sulfate, D-glucose 6-sulfate, D-glucosamine, D-galactosamine, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, D-xylose, D-glucuronic acid
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
requirement, 0.01 M stabilizes the enzyme in a reduced state
plant cysteine oxidases
i.e. PCO dioxygenase, dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets
-
2-mercaptoethanol
-
requirement, 0.1 M, stabilizes the enzyme in a reduced state
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Inhibition of arginyltransferase 1 induces transcriptional activity of myocardin-related transcription factor A (MRTF-A) and promotes directional migration.
Carcinogenesis
MTrasT24, a metallothionein-ras fusion gene, modulates expression in cultured rat liver cells of two genes associated with in vivo liver cancer.
Cardiomegaly
Arginyltransferase knockdown attenuates cardiac hypertrophy and fibrosis through TAK1-JNK1/2 pathway.
Cardiomegaly
Author Correction: Arginyltransferase knockdown attenuates cardiac hypertrophy and fibrosis through TAK1-JNK1/2 pathway.
Cardiomyopathy, Dilated
Contractility of myofibrils from the heart and diaphragm muscles measured with atomic force cantilevers: Effects of heart-specific deletion of arginyl-tRNA-protein transferase.
Heart Failure
Contractility of myofibrils from the heart and diaphragm muscles measured with atomic force cantilevers: Effects of heart-specific deletion of arginyl-tRNA-protein transferase.
Neoplasm Metastasis
Arginyltransferase suppresses cell tumorigenic potential and inversely correlates with metastases in human cancers.
Neoplasm Metastasis
ATE1 Inhibits Liver Cancer Progression through RGS5-Mediated Suppression of Wnt/?-Catenin Signaling.
Neoplasm Metastasis
Reduced Arginyltransferase 1 is a driver and a potential prognostic indicator of prostate cancer metastasis.
Neoplasms
Arginyltransferase suppresses cell tumorigenic potential and inversely correlates with metastases in human cancers.
Neoplasms
ATE1 Inhibits Liver Cancer Progression through RGS5-Mediated Suppression of Wnt/?-Catenin Signaling.
Neoplasms
Comment on "Multiple logistic regression analysis predicts cancer risk among tobacco usage with glutathione R-transferase p1 genotyping in patients with head and neck cancer".
Neoplasms
Multiple competing RNA structures dynamically control alternative splicing in the human ATE1 gene.
Prostatic Neoplasms
Reduced Arginyltransferase 1 is a driver and a potential prognostic indicator of prostate cancer metastasis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
overview: di- and tripeptide inhibitors
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00034
merbromin
Mus musculus
-
in 50 mM HEPES pH 7.5, 25 mM KCl, 15 mM MgCl2, 0.1 mM dithiothreitol, at 37°C
0.00097
Reactive blue 2
Mus musculus
-
in 50 mM HEPES pH 7.5, 25 mM KCl, 15 mM MgCl2, 0.1 mM dithiothreitol, at 37°C
0.00043
suramin
Mus musculus
-
in 50 mM HEPES pH 7.5, 25 mM KCl, 15 mM MgCl2, 0.1 mM dithiothreitol, at 37°C
0.00028
Tannic acid
Mus musculus
-
in 50 mM HEPES pH 7.5, 25 mM KCl, 15 mM MgCl2, 0.1 mM dithiothreitol, at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
specific activity depends on type and age of tissue, picomolar range
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 9.8
-
about half-maximal activity at pH 8.0, about 80% of maximal activity at pH 9.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
gene ATE-1 specifies at least six isoforms which are produced through alternative splicing and are expressed at varying levels in mouse tissues
-
-
brenda
recombinant enzyme, forms Ate1-3 and Ate1-4 of enzyme resulting from alternative splicing are specific for N-terminal Cys residues
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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enhanced ATE1 expression in hypertrophied heart samples, quantitative real-time-PCR expression analysis
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additional information
expression of ATE1 is prominent in the developing brain and spinal cord, and this pattern overlaps with the migration path of neural stem cells
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additional information
ATE protein abundance is spatially and temporally regulated by hormones and light and is highly abundant in meristematic cells
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Ate1 mRNA localized to the tips of the growth cones, likely due to zipcode-mediated targeting. Both ATE1 and arginylated beta-actin are localized at the growth cones
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a small fraction of arginyltransferase 1 localizes within mitochondria
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additional information
additional information
DdAte1-GFP localization in the cytosol and nucleus is more persistent than in transient pseudopodial protruxadsions. DdAte1-GFP expressing cells are measured in nuclei, cytosol, and lamellipodia. DdAte1-GFP is slightly more prominent in cortical protrusions than in the nucleus. Localization analysis of GFP-tagged Ate1, overview
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additional information
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DdAte1-GFP localization in the cytosol and nucleus is more persistent than in transient pseudopodial protruxadsions. DdAte1-GFP expressing cells are measured in nuclei, cytosol, and lamellipodia. DdAte1-GFP is slightly more prominent in cortical protrusions than in the nucleus. Localization analysis of GFP-tagged Ate1, overview
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brenda
additional information
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DdAte1-GFP localization in the cytosol and nucleus is more persistent than in transient pseudopodial protruxadsions. DdAte1-GFP expressing cells are measured in nuclei, cytosol, and lamellipodia. DdAte1-GFP is slightly more prominent in cortical protrusions than in the nucleus. Localization analysis of GFP-tagged Ate1, overview
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brenda
additional information
ATE1 prominently localizes to the growth cones, in addition to the cell bodies. The Ate1 mRNA sequence reveals the existence of putative zipcode-binding sequences involved in mRNA targeting to the cell periphery and local translation at the growth cones
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brenda
additional information
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ATE1 prominently localizes to the growth cones, in addition to the cell bodies. The Ate1 mRNA sequence reveals the existence of putative zipcode-binding sequences involved in mRNA targeting to the cell periphery and local translation at the growth cones
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Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
ATE1 is implicated in cardiovascular development, cancer, neurodegenerative disorders and obesity and can be a potential drug target in management of some of these diseases
evolution
malfunction
metabolism
physiological function
additional information
evolution
the Dictyostelium discoideum genome encodes only one Ate1 family member, Ate1 (DdAte1)
evolution
plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication
evolution
plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication
evolution
plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication
evolution
plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication
evolution
plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication
evolution
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eukaryotic systems including Saccharomyces cerevisiae (budding yeast), mouse cells, and human cells, all contain the evolutionarily conserved ATE1 gene
evolution
plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication
evolution
plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication
evolution
eukaryotic systems including Saccharomyces cerevisiae (budding yeast), mouse cells, and human cells, all contain the evolutionarily conserved ATE1 gene
evolution
eukaryotic systems including Saccharomyces cerevisiae (budding yeast), mouse cells, and human cells, all contain the evolutionarily conserved ATE1 gene
evolution
ATE1 Arg-transferase is an evolutionarily conserved protein present in all eukaryotes from fungi to animals
evolution
arginyltransferase 1 is an evolutionary-conserved eukaryotic protein. A phylogenetic analysis that traces the roots of ATE1 to alpha-proteobacteria, the mitochondrion microbial ancestor
evolution
the enzyme is ubiquitously conserved in eukaryotes. Its evolution is likely accompanied the domestication of mitochondria. ATE1-dependent oxygen-sensing pathway evolves much earlier than the pVHL pathway in molecular evolution
evolution
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eukaryotic systems including Saccharomyces cerevisiae (budding yeast), mouse cells, and human cells, all contain the evolutionarily conserved ATE1 gene
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evolution
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the Dictyostelium discoideum genome encodes only one Ate1 family member, Ate1 (DdAte1)
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evolution
Mus musculus 129SvEv/C57BL/6
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ATE1 Arg-transferase is an evolutionarily conserved protein present in all eukaryotes from fungi to animals
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malfunction
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impairments of arginyltransferase ATE1 are implicated in congenital heart defects, obesity, cancer, and neurodegeneration
malfunction
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diaphragm myofibrils from enzyme-knockout mice produce an increased force compared to myofibrils from wild type
malfunction
conditional knockout mice with Ate1 deletion in the nervous system driven by Nestin promoter (Nes-Ate1 mice) are weaker than wild-type mice, resulting in low postnatal survival rates, and have abnormalities in the brain that suggest defects in neuronal migration. Cultured Ate1 knockout neurons show a reduction in the neurite outgrowth and the levels of doublecortin and F-actin in the growth cones. A lack of beta-actin arginylation leads to a marked reduction in growth cone spreading, accompanied by the corresponding decrease in the actin polymer. Nes-Ate1 mice develope to full term and are born at the expected about 25% ratio, with the body weight and appearance at birth indistinguishable from their wild-type littermates. However, these newborn mice are visibly less active than wild-type, easily pushed away by their littermates during feeding and show no inclination to explore the environment within days after birth. These newborns exhibit dramatically reduced growth in the first days of postnatal life, likely due to their inability to compete for the mother's milk with wild-type littermates. Complete Ate1 knockout mice die at E12.5-E14.5 during development
malfunction
Ate1- null cells are almost completely lacking focal actin adhesion sites at the substrate-attached surface and are only weakly adhesive. In vitro polymerization assays with actin purified from ate1-null cells reveal a diminished polymerization capacity in comparixadson to wild-type actin. Chemotaxis of aggregation-competent ate1-/- null cells is impaired in three-dimensional compared with two-dimensional environments
malfunction
blocking the Arg/N-end rule pathway significantly impaired the fusion of autophagosomes with lysosomes. The inhibition of the Arg/N-end rule pathway with para-chloroamphetamine (PCA) significantly elevates levels of MAPT and huntingtin aggregates, accompanied by increased numbers of LC3 and SQSTM1 puncta. Cells treated with the Arg/N-end rule inhibitor become more sensitized to proteotoxic stress-induced cytotoxicity. Treatment with PCA delays the fusion of autophagosomes with lysosomes and leads to the accumulation of autophagic markers. The direct targets of PCA are UBR1 and UBR2 proteins, not ATE1, an upstream component of the Arg/N-end rule pathway
malfunction
blocking the Arg/N-end rule pathway significantly impaired the fusion of autophagosomes with lysosomes. The inhibition of the Arg/N-end rule pathway with para-chloroamphetamine (PCA) significantly elevates levels of MAPT and huntingtin aggregates, accompanied by increased numbers of LC3 and SQSTM1 puncta. Cells treated with the Arg/N-end rule inhibitor become more sensitized to proteotoxic stress-induced cytotoxicity. Treatment with PCA delays the fusion of autophagosomes with lysosomes and leads to the accumulation of autophagic markers
malfunction
the relative abundance of methylesterase 10 (MES10), nucleoside diphosphate kinase family protein (NDPK1), and two asparagine synthetases (ASNs) is augmented in ate1/ate2 mutants. Disrupted ATE1 in dls1 mutants shows an extremely slow age-dependent, dark-induced leaf senescence, phenotype. Double mutant for AtATE1 and AtATE2 (ate1.ate2) displays lost sensitivity to hormone abscisic acid and consequently uncontrolled seed germination and establishment. Arabidopsis ate1/ate2 or prt6 mutants cannot degrade ERFVII, and as a consequence show increased expression of hypoxia-responsive genes involved in fermentation and sugar consumption even under oxygen-rich conditions
malfunction
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deletion or downregulation of the ATE1 gene disrupts typical stress responses by bypassing growth arrest and suppressing cell death events in the presence of disease-related stressing factors, including oxidative, heat, and osmotic stresses, as well as the exposure to heavy metals or radiation. Conversely, in wild-type cells responding to stress, there is an increase of cellular Ate1 protein level and arginylation activity. The faster growth rates of ate1DELTA mutant yeast in stressing condition compared to wild-type is likely caused by a lack of growth arrest
malfunction
knockout of ATE1 gene in MEFs significantly reduces apoptotic rates in the presence of microbial alkaloid toxin staurosporine (STS) compared to wild-type. Similar results are observed with a different stressor, CdCl2
malfunction
RAP2.12 stabilization in ate1 ate2 double-null mutant plant lines implicates ATE1 as an ERF-VII-targeting arginyl transferase in vivo
malfunction
knockdown of ATE1 does not significantly influence the mRNA expression of unfolded protein response (UPR) proteins, BiP, CHOP, and ATF4
malfunction
deletion of Ate1 in mice leads to embryonic lethality and impairments in multiple physiological systems, including cardiovascular development, angiogenesis, muscle contraction, and cell migration. Lack of arginylation leads to increased Alpha synuclein (alpha-syn) aggregation and causes the formation of larger pathological aggregates in neurons, accompanied by impairments in its ability to be cleared via normal degradation pathways. In the mouse brain, lack of arginylation leads to an increase in alpha-syn's insoluble fraction, accompanied by behavioral changes characteristic for neurodegenerative pathology. Lack of arginylation in the brain leads to neurodegeneration
malfunction
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knockdown of arginyltransferase ATE1 attenuates cardiac hypertrophy and fibrosis in vitro and in vivo through the TAK1-JNK1/2 pathway. The cardioprotective role of ATE1 silencing is mediated by the interruption of TAK1 activity-dependent JNK1/2 signaling pathway. The MAPK signaling cascade is one of the signaling pathways involved in cardiac hypertrophy. ATE1 knockdown in presence of cardiac stress performs a cardioprotective action. Cardiac ATE1 deficiency restores cardiac dysfunction after right renal artery ligation. Phenotype, overview
malfunction
ATE1-null mice show severe intracerebral hemorrhages and cystic space near the neural tubes. The ATE1-/- brain shows defective G-protein signaling. Reduced mitosis in ATE1-/- neuroepithelium and a significantly higher nitric oxide concentration in ATE1-/- brain are observed. In ATE1-null murine embryos, neural-tube genesis is severely defective, and this problem may be the primary cause of embryonic mortality of the mutant mice. ATE1 expression is more prominent in the embryonic brain and spinal cord than in the heart. ATE1-null embryonic brain shows stabilized regulators of G protein signaling (RGS) proteins, defective G protein signaling, and a higher concentration of NO. Proliferation of ATE1-/- neuroepithelial cells in the developing primary neural tube is significantly impaired. Stabilized RGS proteins in ATE1-null mice and reduced activities of downstream effectors, overview
malfunction
arginyltransferase 1 (ATE1) is the only known enzyme in metazoans and fungi that catalyzes posttranslational arginylation. Lack of arginylation is linked to an array of human disorders, including cancer, by altering the response to stress and the regulation of metabolism and apoptosis. The absence of arginyltransferase 1 influences the levels, organization, and function of respiratory chain complexes in mouse cells. ATE1-KO mouse embryonic fibroblasts have increased levels of respiratory supercomplexes I+III2+IVn. However, they have decreased mitochondrial respiration owing to severely lowered complex II levels, which leads to accumulation of succinate and downstream metabolic effects
malfunction
in retinal ON bipolar cells, where regulator of G-protein signaling 7 (RGS7) modulates a G-protein to signal light increments, deletion of arginyltransferase 1 (Ate1) raises the level of RGS7. Electroretinographs reveal that lack of Ate1 leads to increased light-evoked response sensitivities of ON-bipolar cells, as well as their downstream neurons. In cultured mouse embryonic fibroblasts, RGS7 is rapidly degraded via proteasome pathway and this degradation is abolished in Ate1 knockout mouse embryonic fibroblasts
malfunction
the disruption of ATE1 function is implicated in mammalian neurodegenerative disorders and cardiovascular maldevelopment
malfunction
ATE1-KO mouse embryonic fibroblasts (MEFs) acidify the culture media faster than their wild-type counterparts as a sign of enhanced glycolysis. ATE1-KO MEFs show higher rates in glucose intake and lactate production. Similarly, a knockdown of ATE1 expression increases glycolytic rate and capacity
malfunction
ATE1 is implicated in cardiovascular development, cancer, neurodegenerative disorders and obesity
malfunction
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deletion or downregulation of the ATE1 gene disrupts typical stress responses by bypassing growth arrest and suppressing cell death events in the presence of disease-related stressing factors, including oxidative, heat, and osmotic stresses, as well as the exposure to heavy metals or radiation. Conversely, in wild-type cells responding to stress, there is an increase of cellular Ate1 protein level and arginylation activity. The faster growth rates of ate1DELTA mutant yeast in stressing condition compared to wild-type is likely caused by a lack of growth arrest
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malfunction
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Ate1- null cells are almost completely lacking focal actin adhesion sites at the substrate-attached surface and are only weakly adhesive. In vitro polymerization assays with actin purified from ate1-null cells reveal a diminished polymerization capacity in comparixadson to wild-type actin. Chemotaxis of aggregation-competent ate1-/- null cells is impaired in three-dimensional compared with two-dimensional environments
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malfunction
Mus musculus 129SvEv/C57BL/6
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ATE1-null mice show severe intracerebral hemorrhages and cystic space near the neural tubes. The ATE1-/- brain shows defective G-protein signaling. Reduced mitosis in ATE1-/- neuroepithelium and a significantly higher nitric oxide concentration in ATE1-/- brain are observed. In ATE1-null murine embryos, neural-tube genesis is severely defective, and this problem may be the primary cause of embryonic mortality of the mutant mice. ATE1 expression is more prominent in the embryonic brain and spinal cord than in the heart. ATE1-null embryonic brain shows stabilized regulators of G protein signaling (RGS) proteins, defective G protein signaling, and a higher concentration of NO. Proliferation of ATE1-/- neuroepithelial cells in the developing primary neural tube is significantly impaired. Stabilized RGS proteins in ATE1-null mice and reduced activities of downstream effectors, overview
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metabolism
the arginylation branch of the N-end rule pathway positively regulates cellular autophagic flux and clearance of proteotoxic proteins. In the Arg/N-end rule pathway, a main process, that generates a primary destabilizing residue, is the posttranslational conjugation of Arg to pro-N-degrons such as Asp, Glu, and oxidized Cys. This conjugation is solely mediated by ATE1-encoded Arg-tRNA-protein transferase. Arg/N-end rule pathway-dependent degradation of Arg-HSPA5 is a critical regulatory step for autophagosome maturation. Molecular mechanism of Arg/N-end rule dependent autophagic inhibition, oerview
metabolism
the arginylation branch of the N-end rule pathway positively regulates cellular autophagic flux and clearance of proteotoxic proteins. In the Arg/N-end rule pathway, a main process, that generates a primary destabilizing residue, is the posttranslational conjugation of Arg to pro-N-degrons such as Asp, Glu, and oxidized Cys. This conjugation is solely mediated by ATE1-encoded Arg-tRNA-protein transferase. Arg/N-end rule pathway-dependent degradation of Arg-HSPA5 is a critical regulatory step for autophagosome maturation. Molecular mechanism of Arg/N-end rule dependent autophagic inhibition, oerview
metabolism
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. The N-recognin E3 ligase PRT6 and AtATE1 and AtATE2 are involved in seed germination controlled by abscisic acid. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII)
metabolism
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII)
metabolism
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII)
metabolism
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII)
metabolism
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII)
metabolism
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link between Ate1 and a variety of diseases including cancer
metabolism
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII)
metabolism
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII)
metabolism
submergence-induced hypoxia in plants (e.g. flooded plants) results in stabilization of group VII ethylene response factors (ERF-VIIs), which aid survival under these adverse conditions. ERF-VII stability is controlled by the N-end rule pathway, which proposes that ERF-VII N-terminal cysteine oxidation in normoxia enables arginylation followed by proteasomal degradation. The plant cysteine oxidases (PCOs) are identified as catalysts of this oxidation. ERF-VII stabilization in hypoxia presumably arises from reduced PCO activity. PCO dioxygenase activity produces Cys-sulfinic acid at the N-terminus of an ERF-VII peptide, which then undergoes efficient arginylation by an arginyl transferase (ATE1). This provides molecular evidence of N-terminal Cys-sulfinic acid formation and arginylation by N-end rule pathway components, and a substrate of ATE1 in plants. PCOs catalyse dioxygenation of the ERF-VII peptides RAP2_2 to RAP2_11
metabolism
the molecular chaperone BiP (also known as GRP78) is short-lived under basal conditions and endoplasmic reticulum (ER) stress. The turnover of BiP is in part driven by its N-terminal arginylation (Nt-arginylation) by arginyltransferase ATE1, which generates an autophagic N-degron of the N-end rule pathway. ER stress elicits the formation of R-BiP, an effect that is increased when the proteasome is also inhibited. Nt-arginylation correlates with the cytosolic relocalization of BiP under the types of stress tested. The cytosolic relocalization of BiP does not require the functionality of the unfolded protein response or the Sec61- or Derlin1-containing translocon. A key inhibitor of the turnover and Nt-arginylation of BiP is HERP (homocysteine-responsive ER protein), a 43-kDa ER membrane-integrated protein that is an essential component of ER-associated protein degradation. Pharmacological inhibition of the ER-Golgi secretory pathway also suppressed R-BiP formation. Cytosolic R-BiP induced by ER stress and proteasomal inhibition is routed to autophagic vacuoles and possibly additional metabolic fates. These results suggest that Nt-arginylation is a posttranslational modification that modulates the function, localization, and metabolic fate of ER-resident proteins
metabolism
the arginylation branch of the N-end rule pathway is a ubiquitin-mediated proteolytic system in which post-translational conjugation of Arg by ATE1-encoded Arg-tRNA-protein transferase to N-terminal Asp, Glu, or oxidized Cys residues generates essential degradation signals
metabolism
it is possible that ATE1 may be directly or indirectly linked to the alternative function of Arg-tRNA synthetase in RNA editing and potentially other processes in the nucleus. Functional interplay between arginyl-tRNA synthetases and arginyltransferase is decribed
metabolism
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link between Ate1 and a variety of diseases including cancer
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metabolism
Mus musculus 129SvEv/C57BL/6
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the arginylation branch of the N-end rule pathway is a ubiquitin-mediated proteolytic system in which post-translational conjugation of Arg by ATE1-encoded Arg-tRNA-protein transferase to N-terminal Asp, Glu, or oxidized Cys residues generates essential degradation signals
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physiological function
N-terminal arginylation of intracellular proteins by Arg-tRNA-protein transferase is a part of the N-end rule pathway of protein degradation
physiological function
Ate1 plays a role in the regulation of cytoskeleton and is essential for cardiovascular development and angiogenesis
physiological function
posttranslational arginylation mediated by Ate1 is essential for cardiovascular development and angiogenesis and directly affects the myocardium structure in the developing heart
physiological function
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N-terminal arginylation of intracellular proteins by Arg-tRNA-protein transferase is a part of the N-end rule pathway of protein degradation
physiological function
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N-terminal arginylation of intracellular proteins by Arg-tRNA-protein transferase is a part of the N-end rule pathway of protein degradation
physiological function
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posttranslational arginylation mediated by arginyltransferase (ATE1) is an emerging major regulator of embryogenesis and cell physiology
physiological function
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the enzyme is essential for tumor suppression and also participates in suppression of metastatic growth
physiological function
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N-terminal arginylation by the enzyme is essential for coping with cellular stresses caused by excessive misfolded proteins
physiological function
protein arginylation mediated by arginyltransferase ATE1 is an emerging regulatory modification that consists of posttranslational tRNA-mediated addition of arginine to proteins. Arginyltransferase ATE1 regulates embryogenesis and actin cytoskeleton. Role of ATE1 in brain development and neuronal growth. Zipcode-mediated co-targeting of Ate1 and beta-actin mRNA leads to localized co-translational arginylation of beta-actin that drives the growth cone migration and neurite outgrowth. The mechanism that regulates neurite outgrowth during development via arginylation and potentially involves targeted cotranslational arginylation of beta-actin in the developing growth cones, overview. ATE1 is targeted to the tips of the growing neurites where it arginylates beta-actin
physiological function
the highly conserved enzyme arginyl-tRNA-protein transferase (Ate1) mediates arginylation, a posttranslational modification that is only incompletely understood at its molexadcular level. Ate1-mediated posttranslational arginylation affects substrate adhesion and cell migration in Dictyostelium discoideum. Arginylation plays a crucial role in the regulation of cytoskeletal activities
physiological function
arginyltransferases (ATE) mediates N-terminal arginylation of secondary destabilizing residues (D, E, Cox)
physiological function
the Arg/N-end rule pathway may function to actively protect cells from detrimental effects of cellular stresses, including proteotoxic protein accumulation, by positively regulating autophagic flux. Under endplasmic reticulum (ER) stress, ATE1-encoded Arg-tRNA-protein transferases carry out the N-terminal arginylation of the ER heat shock protein HSPA5 that initially targets cargo proteins, along with SQSTM1, to the autophagosome. At the late stage of autophagy, the proteasomal degradation of arginylated HSPA5 might function as a critical checkpoint for the proper progression of autophagic flux in the cells. N-terminal arginylation by ATE1 is usually sufficient for the recognition by UBR proteins and subsequent ubiquitination and degradation in the Arg/N-end rule pathway. The Arg/N-end rule-mediated autophagic flux regulator might be a direct substrate of ATE1, rather than UBR1 or UBR2
physiological function
the Arg/N-end rule pathway may function to actively protect cells from detrimental effects of cellular stresses, including proteotoxic protein accumulation, by positively regulating autophagic flux. Under endplasmic reticulum (ER) stress, ATE1-encoded Arg-tRNA-protein transferases carry out the N-terminal arginylation of the ER heat shock protein HSPA5 that initially targets cargo proteins, along with SQSTM1, to the autophagosome. At the late stage of autophagy, the proteasomal degradation of arginylated HSPA5 might function as a critical checkpoint for the proper progression of autophagic flux in the cells. N-terminal arginylation by ATE1 is usually sufficient for the recognition by UBR proteins and subsequent ubiquitination and degradation in the Arg/N-end rule pathway. The Arg/N-end rule-mediated autophagic flux regulator might be a direct substrate of ATE1, rather than UBR1 or UBR2
physiological function
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu, or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation. In plants, ATE is not required for viability. The arginylation branch of the N-end rule pathway is also responsible for repressing expression of the meristempromoting brevipedicellus (BP) gene during leaf development, acting in a redundant way with the asymmetric leaves 1 (AS1) transcription factor complex, a known negative regulator of BP expression
physiological function
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu, or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation. In plants, ATE is not required for viability
physiological function
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu, or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation. In plants, ATE is not required for viability
physiological function
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu, or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation. In plants, ATE is not required for viability
physiological function
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation
physiological function
-
arginyltransferase 1 (Ate1) mediates protein arginylation, a protein posttranslational modification (PTM) in eukaryotic cells. Ate1 is required to suppress mutation frequency in yeast and mammalian cells during DNA-damaging conditions such as ultraviolet irradiation. Ate1 and arginylation are upregulated during stress and are responsible for cell death, role of Ate1/arginylation in stress response, overview. Ate1 is essential for the suppression of mutagenesis during DNA-damaging stress. Growth arrest and cell death during stress could be interpreted as a mechanism to prevent incorporation of damaged genetic material or transmission of mutation to the subsequent generations
physiological function
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu, or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation
physiological function
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu, or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation
physiological function
arginyltransferase 1 (Ate1) mediates protein arginylation, a protein posttranslational modification (PTM) in eukaryotic cells. Ate1 is required to suppress mutation frequency in yeast and mammalian cells during DNA-damaging conditions such as ultraviolet irradiation. Ate1 and arginylation are upregulated during stress and are responsible for cell death, role of Ate1/arginylation in stress response, overview. Ate1 is essential for the suppression of mutagenesis during DNA-damaging stress. Growth arrest and cell death during stress could be interpreted as a mechanism to prevent incorporation of damaged genetic material or transmission of mutation to the subsequent generations
physiological function
arginyltransferase 1 (Ate1) mediates protein arginylation, a protein posttranslational modification (PTM) in eukaryotic cells. Ate1 is required to suppress mutation frequency in yeast and mammalian cells during DNA-damaging conditions such as ultraviolet irradiation. Ate1 and arginylation are upregulated during stress and are responsible for cell death, role of Ate1/arginylation in stress response, overview. Ate1 is essential for the suppression of mutagenesis during DNA-damaging stress. Growth arrest and cell death during stress could be interpreted as a mechanism to prevent incorporation of damaged genetic material or transmission of mutation to the subsequent generations
physiological function
PCO dioxygenase activity produces Cys-sulfinic acid at the N-terminus of an ERF-VII peptide, which then undergoes efficient arginylation by an arginyl transferase (ATE1). This provides molecular evidence of N-terminal Cys-sulfinic acid formation and arginylation by N-end rule pathway components, and a substrate of ATE1 in plants. Proposed arginylation requirements for the Arg/Cys branch of the N-end rule pathway
physiological function
N-terminal arginylation (Nt-arginylation) is a posttranslational modification for which the amino acid L-Arg is conjugated to the Nt-Asp or Nt-Glu residues by ATE1-encoded R-transferases. Nt-arginylation is a posttranslational modification that modulates the function, localization, and metabolic fate of endoplasmic reticulum (ER)-resident proteins. A set of ER-residing molecular chaperones, such as BiP, calreticulin, and PDI, are N-terminally arginylated by enzyme ATE1. Nt-arginylation of BiP is induced in response to cytosolic double-stranded DNA, leading to the cytosolic accumulation of Nt-arginylated BiP, R-BiP. The Nt-Arg residue of R-BiP binds p62 (also known as SQSTM1 and Sequestosome-1) and subsequently is delivered to the autophagosomes for lysosomal degradation. Nt-arginylation mediates the cytosolic relocalization of BiP independently of the functionality of the ERAD core machinery
physiological function
protein arginylation is a posttranlsational modification mediated by arginyltransferase ATE1 that transfers Arg from tRNA directly to protein targets. Protein arginylation targets alpha-synuclein, facilitates normal brain health, and prevents neurodegeneration. Alpha-synuclein (alpha-syn) is a central player in neurodegeneration. It is a highly efficient substrate for arginyltransferase ATE1 and is arginylated in vivo by a mid-chain mechanism that targets the acidic side chains of E46 and E83. alpha-Syn arginylation can be a factor that facilitates normal alpha-syn folding and function in vivo. Arginylation reduces aggregation of pre-formed alpha-syn fibrils and partially prevents alpha-syn-induced seeding of pathological aggregates in cultured neurons, overview
physiological function
-
arginyltransferase ATE1 can modulate the hypertrophic growth of myocytes induced by Ang II. Physiological importance of ATE1 in higher eukaryotes
physiological function
protein arginylation, mediated by the arginyltransferase ATE1, is a posttranslational modification that is essential for mammalian embryogenesis, regulates many fundamental biological processes, and targets a large number of proteins in vivo. In mammals, ATE1 is represented by four homologous isoforms ATE1-1, 2, 3, and 4, generated by alternative splicing from a single gene and reported in different studies to have varying activity, substrate specificity, and tissue-specific expression. In addition to N-terminal arginylation, ATE1 can also add arginine to the acidic side chains of Asp and Glu on the mid-chain sites of intact proteins
physiological function
ATE1 Arg-transferase is the key enzyme in the Arg/N-end rule pathway. ATE1 is required for degradation of regulators of G protein signaling (RGS) proteins and GPCR signaling, regulation, overview. Essential role of N-terminal arginylation in neural tube development. The crucial role of ATE1 in neural tube development is directly related to proper turn-over of the RGS4 protein, which participate in the oxygen-sensing mechanism in the cells. Degradation of the RGS4 protein by ATE1 is closely associated with the migration or differentiation of neural crest cells during embryogenesis. Neural crest cells migrate into the heart and vessels
physiological function
the enzyme transfers the amino acid arginine from Arg-tRNAArg to the N-terminal residues of proteins, such as aspartate, glutamate, and oxidized cysteine. The resulting N-terminal-Arg acts as an N-degron that regulates the degradation of various biomaterials via the ubiquitin/Ub-proteasome system (UPS) or the autophagy-lysosome system (ALS)
physiological function
arginyltransferase 1 (ATE1) is the only known enzyme in metazoans and fungi that catalyzes posttranslational arginylation. Role of of arginyltransferase 1 in the regulation of mitochondrial and cellular energy metabolism. ATE1 may affect the mitochondrial import and/or assembly of succinate dehydrogenase subunits, ultimately leading to complex II deficiency. ATE1 may play an instrumental role in contributing to the metabolic shift from OXPHOS to glycolysis seen in cancer and inflammation, and the adaptation to oxidative, hypoxic, or thermal stresses
physiological function
eukaryotic post-translational arginylation, mediated by the family of enzymes known as the arginyltransferases (ATE1s), is an important post-translational modification that can alter protein function and even dictate cellular protein half-life
physiological function
arginyl-transferase ATE1 is a tRNA-dependent enzyme that covalently attaches an arginine molecule to a protein substrate
physiological function
arginyltransferase 1 (Ate1) regulates RGS7 levels by directly or indirectly facilitating proteasomal degradation of regulator of G-protein signaling 7 (RGS7) in vivo and thus regulates RGS7-dependent G-protein signaling in the nervous system
physiological function
arginyltransferase 1 (ATE1) catalyzes arginylation, an important posttranslational modification (PTM) in eukaryotes that plays a critical role in cellular homeostasis
physiological function
ATE1 controls glycolysis and hypoxic response in mammalian cells by affecting HIF1alpha. HIF1alpha is arginylated by ATE1 and degraded by UBRs independently of pVHL. ATE1/UBR and pVHL pathways jointly regulate oxygen sensing in a transcription-independent manner with different tissue specificities
physiological function
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arginyltransferase 1 mediates proteasomal degradation of viral haemagglutinin protein. This is a unique host defence mechanism
physiological function
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arginyltransferase 1 (Ate1) mediates protein arginylation, a protein posttranslational modification (PTM) in eukaryotic cells. Ate1 is required to suppress mutation frequency in yeast and mammalian cells during DNA-damaging conditions such as ultraviolet irradiation. Ate1 and arginylation are upregulated during stress and are responsible for cell death, role of Ate1/arginylation in stress response, overview. Ate1 is essential for the suppression of mutagenesis during DNA-damaging stress. Growth arrest and cell death during stress could be interpreted as a mechanism to prevent incorporation of damaged genetic material or transmission of mutation to the subsequent generations
-
physiological function
-
eukaryotic post-translational arginylation, mediated by the family of enzymes known as the arginyltransferases (ATE1s), is an important post-translational modification that can alter protein function and even dictate cellular protein half-life
-
physiological function
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the highly conserved enzyme arginyl-tRNA-protein transferase (Ate1) mediates arginylation, a posttranslational modification that is only incompletely understood at its molexadcular level. Ate1-mediated posttranslational arginylation affects substrate adhesion and cell migration in Dictyostelium discoideum. Arginylation plays a crucial role in the regulation of cytoskeletal activities
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physiological function
Mus musculus 129SvEv/C57BL/6
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ATE1 Arg-transferase is the key enzyme in the Arg/N-end rule pathway. ATE1 is required for degradation of regulators of G protein signaling (RGS) proteins and GPCR signaling, regulation, overview. Essential role of N-terminal arginylation in neural tube development. The crucial role of ATE1 in neural tube development is directly related to proper turn-over of the RGS4 protein, which participate in the oxygen-sensing mechanism in the cells. Degradation of the RGS4 protein by ATE1 is closely associated with the migration or differentiation of neural crest cells during embryogenesis. Neural crest cells migrate into the heart and vessels
-
additional information
GFP-tagged Ate1 rapidly relocates to sites of newly formed actin-rich protrusions
additional information
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GFP-tagged Ate1 rapidly relocates to sites of newly formed actin-rich protrusions
additional information
identification of targets and interaction partners, e.g. sHSP17.2a chaperone, of arginyl-tRNA protein transferase (ATE) in the model plant Physcomitrella patens by mass spectrometry, employing two different immunoaffinity strategies and a recently established transgenic ATE:GUS reporter line. A commercially available antibody against the fused reporter protein (beta-glucuronidase) to pull down ATE and its interacting proteins. Preparation of specific antibodies and immunoprecipitation of arginylated proteins, overview. Arginylated peptides are reliably identified for three different proteins namely acylamino-acid releasing enzyme (PpAARE, Pp1s619_3V6.1), an uncharacterized protein (UP, Pp1s68_62V6.1) and a putative AAA-type ATPase (PpATAD3.1, Pp1s106_174V6.1), and for one additional protein, an ABC transporter family protein (PpABCB20, Pp1s29_108V6.1). The identified arginylation do not represent a side-chain arginylation as the a1 ion of a dimethylated arginine is present in the corresponding HCD spectrum
additional information
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identification of targets and interaction partners, e.g. sHSP17.2a chaperone, of arginyl-tRNA protein transferase (ATE) in the model plant Physcomitrella patens by mass spectrometry, employing two different immunoaffinity strategies and a recently established transgenic ATE:GUS reporter line. A commercially available antibody against the fused reporter protein (beta-glucuronidase) to pull down ATE and its interacting proteins. Preparation of specific antibodies and immunoprecipitation of arginylated proteins, overview. Arginylated peptides are reliably identified for three different proteins namely acylamino-acid releasing enzyme (PpAARE, Pp1s619_3V6.1), an uncharacterized protein (UP, Pp1s68_62V6.1) and a putative AAA-type ATPase (PpATAD3.1, Pp1s106_174V6.1), and for one additional protein, an ABC transporter family protein (PpABCB20, Pp1s29_108V6.1). The identified arginylation do not represent a side-chain arginylation as the a1 ion of a dimethylated arginine is present in the corresponding HCD spectrum
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
additional information
estimation of the scope and evolutionary conservation of the N-terminal arginylome, analysis to a shorter list of likely arginylation targets with likely conserved regulation across mammals, these protein targets may be highly regulated by N-terminal arginylation in vivo, overview
additional information
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estimation of the scope and evolutionary conservation of the N-terminal arginylome, analysis to a shorter list of likely arginylation targets with likely conserved regulation across mammals, these protein targets may be highly regulated by N-terminal arginylation in vivo, overview
additional information
-
GFP-tagged Ate1 rapidly relocates to sites of newly formed actin-rich protrusions
-
Show AA Sequence and Transmembrane Helices (4633 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
360000
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multienzyme complex of several molecules of arginyl-tRNA synthetase and arginyl-tRNA-protein transferase, gel filtration
60000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
additional information
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
additional information
domain architecture of DdAte1 and structure comparisons, overview
additional information
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domain architecture of DdAte1 and structure comparisons, overview
additional information
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domain architecture of DdAte1 and structure comparisons, overview
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additional information
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multienzyme complex of several molecules of arginyl-tRNA synthetase and arginyl-tRNA-protein transferase
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
additional information
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interaction of enzyme and N-terminal domain of topoisomerase II
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of native and SeMet-substituted ATE1 are obtained by sitting-drop vapor-diffusion
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K476E/R477E
cells with the K476E/R477E mutant show significant inhibition of RGS4 proteasomal flux
K88E/K92E
the mutant shows about a 2fold reduction in binding affinity to the A + T arms compared to the DELTA191-220 variant
W38F/H40E/K476E
substantial difference in RGS4 interaction with the triple mutant W38F/H40E/K476E compared to the wild-type enzyme
W38F/H40E/K476E/R477E
cells with the W38F/H40E/K476E/R477E mutant show significant inhibition of RGS4 proteasomal flux
malfunction
knockout of ATE1 gene in MEFs significantly reduces apoptotic rates in the presence of microbial alkaloid toxin staurosporine (STS) compared to wild-type. Similar results are observed with a different stressor, CdCl2
Y416A
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no effect on Asp-containing substrate, but affects Glu-containing substrate
additional information
additional information
generation of RAP2.12 stabilization in ate1 ate2 double-null mutant plant lines
additional information
knockout of the gene encoding Ate1 and analysis of ate1- null cell phenotype, overview. Actin cytoskeleton dynamics by live-cell microscopy indicated significant changes in comparison to wild-type cells. In two-dimensional chemotaxis assays toward folate or cAMP, the motility of ate1-null cells is increased, while in three-dimensional chemoxadtaxis involving more confined conditions, the motility of ate1-null cells is significantly rexadduced. Actin isolated from ate1-null cells reveals different isoelectric properties and lower polymerization capacity in comparison to actin from wild-type
additional information
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knockout of the gene encoding Ate1 and analysis of ate1- null cell phenotype, overview. Actin cytoskeleton dynamics by live-cell microscopy indicated significant changes in comparison to wild-type cells. In two-dimensional chemotaxis assays toward folate or cAMP, the motility of ate1-null cells is increased, while in three-dimensional chemoxadtaxis involving more confined conditions, the motility of ate1-null cells is significantly rexadduced. Actin isolated from ate1-null cells reveals different isoelectric properties and lower polymerization capacity in comparison to actin from wild-type
additional information
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knockout of the gene encoding Ate1 and analysis of ate1- null cell phenotype, overview. Actin cytoskeleton dynamics by live-cell microscopy indicated significant changes in comparison to wild-type cells. In two-dimensional chemotaxis assays toward folate or cAMP, the motility of ate1-null cells is increased, while in three-dimensional chemoxadtaxis involving more confined conditions, the motility of ate1-null cells is significantly rexadduced. Actin isolated from ate1-null cells reveals different isoelectric properties and lower polymerization capacity in comparison to actin from wild-type
-
additional information
construction of a conditional mouse ATE1 knockout model (Ate1-floxed mice), phenotype, overview. Complete Ate1 knockout mice die at E12.5-E14.5 during development. Nes-Ate1 mice develope to full term and are born at the expected about 25% ratio, with the body weight and appearance at birth indistinguishable from their wild-type littermates. However, these newborn mice are visibly less active than wild-type, easily pushed away by their littermates during feeding and show no inclination to explore the environment within days after birth. These newborns exhibit dramatically reduced growth in the first days of postnatal life, likely due to their inability to compete for the mother's milk with wild-type littermates. Brain phenotypes, overview. Lack of arginylation causes defects in neurite outgrowth
additional information
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construction of a conditional mouse ATE1 knockout model (Ate1-floxed mice), phenotype, overview. Complete Ate1 knockout mice die at E12.5-E14.5 during development. Nes-Ate1 mice develope to full term and are born at the expected about 25% ratio, with the body weight and appearance at birth indistinguishable from their wild-type littermates. However, these newborn mice are visibly less active than wild-type, easily pushed away by their littermates during feeding and show no inclination to explore the environment within days after birth. These newborns exhibit dramatically reduced growth in the first days of postnatal life, likely due to their inability to compete for the mother's milk with wild-type littermates. Brain phenotypes, overview. Lack of arginylation causes defects in neurite outgrowth
additional information
generation of Ate1 knockout mice and Ate1 knockout mouse embryonic fibroblasts, phenotypes, overview. alpha-Syn-transfected Ate1 knockout cells are treated with chloroquine and bafilomycin, the inhibitors of lysosomal degradation and autophagy previously shown to interfere with alpha-syn removal from normal cells. Neither of these treatments in Ate1 knockout leads to the expected increase in intracellular levels of alpha-syn, suggesting that neither lysosomal degradation nor autophagy contribute substantially to the removal of alpha-syn, in the absence of arginylation
additional information
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generation of Ate1 knockout mice and Ate1 knockout mouse embryonic fibroblasts, phenotypes, overview. alpha-Syn-transfected Ate1 knockout cells are treated with chloroquine and bafilomycin, the inhibitors of lysosomal degradation and autophagy previously shown to interfere with alpha-syn removal from normal cells. Neither of these treatments in Ate1 knockout leads to the expected increase in intracellular levels of alpha-syn, suggesting that neither lysosomal degradation nor autophagy contribute substantially to the removal of alpha-syn, in the absence of arginylation
additional information
generation of ATE1-/- deletion mice. Genotyping of litter embryos at E14.5 retrieved from the ATE+/- intercross reveals no live homozygous mutants, indicating that the deletion of the ATE1 gene is lethal at midgestation. Defective neuronal-cell proliferation in the ATE1-null embryonic brain, overview
additional information
Mus musculus 129SvEv/C57BL/6
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generation of ATE1-/- deletion mice. Genotyping of litter embryos at E14.5 retrieved from the ATE+/- intercross reveals no live homozygous mutants, indicating that the deletion of the ATE1 gene is lethal at midgestation. Defective neuronal-cell proliferation in the ATE1-null embryonic brain, overview
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additional information
ATE abundance underlies spatiotemporal patterning in the moss Physcomitrella patens using a translational GUS reporter fusion via knock-in at the endogenous genomic locus. The tagged version of ATE is used to pull down specifically ATE together with potential interaction partners from tissues where ATE abundance is monitored via histochemical GUS staining
additional information
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ATE abundance underlies spatiotemporal patterning in the moss Physcomitrella patens using a translational GUS reporter fusion via knock-in at the endogenous genomic locus. The tagged version of ATE is used to pull down specifically ATE together with potential interaction partners from tissues where ATE abundance is monitored via histochemical GUS staining
additional information
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for the generation of ATE1 knockdown hypertrophied rats, ATE1 siRNA is encapsulated in stearic acid-modified carboxy methyl chitosan (CMC) conjugated to a cardiomyocyte-targeting peptide. Cardiac function is improved in terms of left ventricular diastolic dysfunction (LVDd) and fractional shortening (%FS) in the ligated + ATE1-siRNA as compared to the Ligated + NS-siRNA when examined by M-Mode echocardiography. Cardiac ATE1 deficiency restores cardiac dysfunction after right renal artery ligation. ATE1 knockdown H9C2 cells
additional information
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knockout or knockdown of ATE1 decreasing cellular sensitivity towards stressing conditions, e.g. heat, high NaCl, or H2O2
additional information
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knockout or knockdown of ATE1 decreasing cellular sensitivity towards stressing conditions, e.g. heat, high NaCl, or H2O2
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol, 20%, stabilizes concentrated enzyme solutions during storage
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polyethylene glycol, 30%, stabilizes concentrated solutions during storage
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, concentrated enzyme solution, 20% glycerol, t1/2: about 1 week
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4°C, concentrated enzyme solution, 0.5 M phosphate-KOH-buffer, pH 7.8, 0.1 M 2-mercaptoethanol, up to 6 months
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4°C, purified, 0.05 M Tris-HCl buffer, pH 8.0, 0.1 M 2-mercaptoethanol, 0.09 M KCl, 0.02 M spermine, 1 week
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on heparin-Sepharose and angiotensin II-Sepharose combined with affinity elution with lactalbumin
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recombinant N-terminally His6-tagged enzyme ATE1 from Escherichia coli strain BL21-CodonPlus (DE3)-RIL by nickel affinity chromatography, tag cleavage by TEV protease, and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a targeting vector is constructed to generate Ate1-deficient mice
expression in Escherichia coli
gene ATE1 or At5g05700, sequence comparisons, phylogenetic analysis and domain location of ATE protein sequences among plant species
gene ATE1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant C-terminal GFP-tagged DdAte1 is transxadfected into Dictyostelium wild-type cells, it localizes to the cytosol and is enriched in the nucleus and pseudopodial protruxadsions
gene ATE1, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIL
gene ate1, single copy gene
gene ATE1_1, phylogenetic analysis and domain location of ATE protein sequences among plant species
gene CHLRE_13g580600v5, phylogenetic analysis and domain location of ATE protein sequences among plant species
gene Os05g0446800, phylogenetic analysis and domain location of ATE protein sequences among plant species
gene PHYPA_004926, phylogenetic analysis and domain location of ATE protein sequences among plant species
gene POPTR_010G190100, phylogenetic analysis and domain location of ATE protein sequences among plant species
gene SORBI_3009G156000, phylogenetic analysis and domain location of ATE protein sequences among plant species
mouse genomic DNA encoding Ate1 is isolated from a BAC library, Ate1-deficient mouse strains are constructed
a targeting vector is constructed to generate Ate1-deficient mice
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ATE abundance is increased in moss (Physcomitrella patens) leafy gametophores after application of the stress hormone abscisic acid (ABA), in darkness or in red light, using a translational ATE:GUS fusion at the endogenous locus
Ate1 and arginylation are upregulated during stress and are responsible for cell death, stress is caused by e.g. H2O2, CdCl2, heat, high salt, or staurosporine, overview
Ate1 and arginylation are upregulated during stress and are responsible for cell death, stress is caused by e.g. H2O2, CdCl2, heat, high salt, or staurosporine. In wild-type cells responding to stress, there is an increase of cellular Ate1 protein level and arginylation activity, overview. The increase of Ate1 protein directly promotes cell death in a manner dependent on its arginylation activity. The wild-type and ate1DELTA yeast are challenged with high-temperature conditions: at 40C, a heat-stress temperature for yeast, the mutant ate1DELTA yeast grows significantly faster than the wild-type. Buut when these yeast cultures are transferred from 40C to room temperature, a non-stressing temperature for recovery, similar numbers of colonies eventually form in both the ate1DELTA and wild-type yeast. This suggests that both yeast strains are equally viable, and their difference in growth at 40C is mainly due to a difference in growth arrest
ATE1 expression is upregulated by hypertrophic stimuli, increase in ATE1 expression upon hypertrophic stress
-
ATE1 mRNA expression is increased from 1.0fold to 1.8fold and 2.0fold after 48 and 72 h of Newcastle disease virus infection, respectively
-
enzyme expression is 2fold induced after 3 days and 7-8fold after 7 days of auxin application
-
the enzyme is downregulated in several types of human cancer samples at the protein level
-
Ate1 and arginylation are upregulated during stress and are responsible for cell death, stress is caused by e.g. H2O2, CdCl2, heat, high salt, or staurosporine, overview
Ate1 and arginylation are upregulated during stress and are responsible for cell death, stress is caused by e.g. H2O2, CdCl2, heat, high salt, or staurosporine, overview
Ate1 and arginylation are upregulated during stress and are responsible for cell death, stress is caused by e.g. H2O2, CdCl2, heat, high salt, or staurosporine. In wild-type cells responding to stress, there is an increase of cellular Ate1 protein level and arginylation activity, overview. The increase of Ate1 protein directly promotes cell death in a manner dependent on its arginylation activity. The wild-type and ate1DELTA yeast are challenged with high-temperature conditions: at 40C, a heat-stress temperature for yeast, the mutant ate1DELTA yeast grows significantly faster than the wild-type. Buut when these yeast cultures are transferred from 40C to room temperature, a non-stressing temperature for recovery, similar numbers of colonies eventually form in both the ate1DELTA and wild-type yeast. This suggests that both yeast strains are equally viable, and their difference in growth at 40C is mainly due to a difference in growth arrest
-
Ate1 and arginylation are upregulated during stress and are responsible for cell death, stress is caused by e.g. H2O2, CdCl2, heat, high salt, or staurosporine. In wild-type cells responding to stress, there is an increase of cellular Ate1 protein level and arginylation activity, overview. The increase of Ate1 protein directly promotes cell death in a manner dependent on its arginylation activity. The wild-type and ate1DELTA yeast are challenged with high-temperature conditions: at 40C, a heat-stress temperature for yeast, the mutant ate1DELTA yeast grows significantly faster than the wild-type. Buut when these yeast cultures are transferred from 40C to room temperature, a non-stressing temperature for recovery, similar numbers of colonies eventually form in both the ate1DELTA and wild-type yeast. This suggests that both yeast strains are equally viable, and their difference in growth at 40C is mainly due to a difference in growth arrest
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
plant cysteine oxidases (PCOs) and enzyme ATE1 may be viable intervention targets to stabilize N-end rule substrates, including ERF-VIIs, to enhance submergence tolerance in agriculture
medicine
medicine
-
arginyltransferase inversely correlates with metastases in human cancers and patient survival
medicine
-
the inhibition of ATE1 activity may provide an approach for the treatment of cardiac hypertrophy in humans
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Deutch, C.E.
Aminoacyl-tRNA: protein transferases
Methods Enzymol.
106
198-205
1984
Oryctolagus cuniculus
brenda
Soffer, R.L.; Horinishi, H.
Enzymic modification of proteins. I. General characteristics of the arginine-transfer reaction in rabbit liver cytoplasm
J. Mol. Biol.
43
163-175
1969
Oryctolagus cuniculus
brenda
Soffer, R.L.
Enzymatic modification of proteins. II. Purification and properties of the arginyl transfer ribonucleic acid-protein transferase from rabbit liver cytoplasm
J. Biol. Chem.
245
731-737
1970
Oryctolagus cuniculus
brenda
Soffer, R.L.
Peptide acceptors in the arginine transfer reaction
J. Biol. Chem.
248
2918-2921
1973
Oryctolagus cuniculus
brenda
Kato, M.
Heparin as an inhibitor of L-arginyl-tRNA: protein arginyltransferase
J. Biochem.
94
2015-2022
1983
Sus scrofa, Rattus norvegicus, Saccharomyces cerevisiae
brenda
Kato, M.; Nozawa, Y.
Complete purification of arginyl-tRNA:protein arginyltransferase from hog kidney and production of its antibody
Anal. Biochem.
143
361-367
1984
Sus scrofa
brenda
Ciechanover, A.; Ferber, S.; Ganoth, D.; Elias, S.; Avram, H.; Arfin, S.
Purification and characterization of arginyl-tRNA-protein transferase from rabbit reticulocytes. Its involvement in post-translational modification and degradation of acidic NH2 termini substrates of the ubiquitin pathway
J. Biol. Chem.
263
11155-11167
1988
Oryctolagus cuniculus
brenda
Soffer, R.L.
The arginine transfer reaction
Biochim. Biophys. Acta
155
228-240
1968
Ovis aries
brenda
Kaji, H.
Amino-terminal arginylation of chromosomal proteins by arginyl-tRNA
Biochemistry
15
5121-5125
1976
Mus musculus, Mus musculus BALB/c
brenda
Kaji, H.; Novelli, G.D.; Kaji, A.
A soluble amino acid incorporation system from rat liver
Biochim. Biophys. Acta
76
474-477
1963
Rattus norvegicus
brenda
Kwon, Y.T.; Kashina, A.S.; Davydov, I.V.; Hu, R.G.; An, J.Y.; Seo, J.W.; Du, F.; Varshavsky, A.
An essential role of N-terminal arginylation in cardiovascular development
Science
297
96-99
2002
Mus musculus
brenda
Kwon, Y.T.; Kashina, A.S.; Varshavsky, A.
Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway
Mol. Cell. Biol.
19
182-193
1999
Homo sapiens (O95260), Homo sapiens, Mus musculus (Q9Z2A5), Mus musculus
brenda
Li, J.; Pickart, C.M.
Inactivation of arginyl-tRNA protein transferase by a bifunctional arsenoxide: Identification of residues proximal to the arsenoxide site
Biochemistry
34
139-147
1995
Saccharomyces cerevisiae
brenda
Takao, K.; Samejima, K.
Arginyl-tRNA-protein transferase activities in crude supernatants of rat tissues
Biol. Pharm. Bull.
22
1007-1009
1999
Rattus norvegicus
brenda
Takao, K.; Xu, Y.J.; Samejima, K.; Shirahata, A.; Nitsu, M.
Preparation and usefulness of some fluorogenic substrates for assay of arginyl-tRNA-Protein transferase by HPLC
Anal. Biochem.
267
373-381
1999
Sus scrofa
brenda
Yoshida, S.; Ito, M.; Callis, J.; Nishida, I.; Watanabe, A.
A delayed leaf senescence mutant is defective in arginyl-tRNA: protein arginyltransferase, a component of the N-end rule pathway in Arabidopsis
Plant J.
32
129-137
2002
Arabidopsis thaliana
brenda
Barker, C.R.; Mouchel, N.A.; Jenkins, J.R.
The identification and characterisation of a functional interaction between arginyl-tRNA-protein transferase and topoisomerase II
Biochem. Biophys. Res. Commun.
342
596-604
2006
Saccharomyces cerevisiae
brenda
Rai, R.; Mushegian, A.; Makarova, K.; Kashina, A.
Molecular dissection of arginyltransferases guided by similarity to bacterial peptidoglycan synthases
EMBO Rep.
7
800-805
2006
Mus musculus
brenda
Hu, R.G.; Brower, C.S.; Wang, H.; Davydov, I.V.; Sheng, J.; Zhou, J.; Kwon, Y.T.; Varshavsky, A.
Arginyltransferase, its specificity, putative substrates, bidirectional promoter, and splicing-derived isoforms
J. Biol. Chem.
281
32559-32573
2006
Mus musculus
brenda
Decca, M.B.; Bosc, C.; Luche, S.; Brugiere, S.; Job, D.; Rabilloud, T.; Garin, J.; Hallak, M.E.
Protein arginylation in rat brain cytosol: a proteomic analysis
Neurochem. Res.
31
401-409
2006
Rattus norvegicus
brenda
Rai, R.; Kashina, A.
Identification of mammalian arginyltransferases that modify a specific subset of protein substrates
Proc. Natl. Acad. Sci. USA
102
10123-10128
2005
Mus musculus
brenda
Rai, R.; Wong, C.C.; Xu, T.; Leu, N.A.; Dong, D.W.; Guo, C.; McLaughlin, K.J.; Yates, J.R.; Kashina, A.
Arginyltransferase regulates alpha cardiac actin function, myofibril formation and contractility during heart development
Development
135
3881-3889
2008
Mus musculus (Q9Z2A5), Mus musculus
brenda
Leu, N.A.; Kurosaka, S.; Kashina, A.
Conditional Tek promoter-driven deletion of arginyltransferase in the germ line causes defects in gametogenesis and early embryonic lethality in mice
PLoS ONE
4
e7734
2009
Mus musculus (Q9Z2A5), Mus musculus
brenda
Brower, C.S.; Varshavsky, A.
Ablation of arginylation in the mouse N-end rule pathway: loss of fat, higher metabolic rate, damaged spermatogenesis, and neurological perturbations
PLoS ONE
4
e7757
2009
Mus musculus (Q9Z2A5), Mus musculus
brenda
Hu, R.; Wang, H.; Xia, Z.; Varshavsky, A.
The N-end rule pathway is a sensor of heme
Proc. Natl. Acad. Sci. USA
105
76-81
2008
Mus musculus, Saccharomyces cerevisiae
brenda
Holman, T.J.; Jones, P.D.; Russell, L.; Medhurst, A.; Ubeda Tomas, S.; Talloji, P.; Marquez, J.; Schmuths, H.; Tung, S.A.; Taylor, I.; Footitt, S.; Bachmair, A.; Theodoulou, F.L.; Holdsworth, M.J.
The N-end rule pathway promotes seed germination and establishment through removal of ABA sensitivity in Arabidopsis
Proc. Natl. Acad. Sci. USA
106
4549-4554
2009
Arabidopsis thaliana (Q9ZT48), Arabidopsis thaliana
brenda
Saha, S.; Wang, J.; Buckley, B.; Wang, Q.; Lilly, B.; Chernov, M.; Kashina, A.
Small molecule inhibitors of arginyltransferase regulate arginylation-dependent protein degradation, cell motility, and angiogenesis
Biochem. Pharmacol.
83
866-873
2012
Mus musculus
brenda
Wang, J.; Han, X.; Saha, S.; Xu, T.; Rai, R.; Zhang, F.; Wolf, Y.I.; Wolfson, A.; Yates, J.R.; Kashina, A.
Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo
Chem. Biol.
18
121-130
2011
Mus musculus
brenda
Wang, J.; Han, X.; Wong, C.C.; Cheng, H.; Aslanian, A.; Xu, T.; Leavis, P.; Roder, H.; Hedstrom, L.; Yates, J.R.; Kashina, A.
Arginyltransferase ATE1 catalyzes midchain arginylation of proteins at side chain carboxylates in vivo
Chem. Biol.
21
331-337
2014
Mus musculus
brenda
Carpio, M.A.; Decca, M.B.; Lopez Sambrooks, C.; Durand, E.S.; Montich, G.G.; Hallak, M.E.
Calreticulin-dimerization induced by post-translational arginylation is critical for stress granules scaffolding
Int. J. Biochem. Cell Biol.
45
1223-1235
2013
Mus musculus
brenda
Ribeiro, P.A.; Ribeiro, J.P.; Minozzo, F.C.; Pavlov, I.; Leu, N.A.; Kurosaka, S.; Kashina, A.; Rassier, D.E.
Contractility of myofibrils from the heart and diaphragm muscles measured with atomic force cantilevers: effects of heart-specific deletion of arginyl-tRNA-protein transferase
Int. J. Cardiol.
168
3564-3571
2013
Mus musculus
brenda
Cha-Molstad, H.; Sung, K.S.; Hwang, J.; Kim, K.A.; Yu, J.E.; Yoo, Y.D.; Jang, J.M.; Han, D.H.; Molstad, M.; Kim, J.G.; Lee, Y.J.; Zakrzewska, A.; Kim, S.H.; Kim, S.T.; Kim, S.Y.; Lee, H.G.; Soung, N.K.; Ahn, J.S.; Ciechanover, A.; Kim, B.Y.; Kwon, Y.T.
Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding
Nat. Cell Biol.
17
917-929
2015
Mus musculus
brenda
Schuessele, C.; Hoernstein, S.N.; Mueller, S.J.; Rodriguez-Franco, M.; Lorenz, T.; Lang, D.; Igloi, G.L.; Reski, R.
Spatio-temporal patterning of arginyl-tRNA protein transferase (ATE) contributes to gametophytic development in a moss
New Phytol.
209
1014-1027
2016
Physcomitrium patens
brenda
Rai, R.; Zhang, F.; Colavita, K.; Leu, N.A.; Kurosaka, S.; Kumar, A.; Birnbaum, M.D.; Gyorffy, B.; Dong, D.W.; Shtutman, M.; Kashina, A.
Arginyltransferase suppresses cell tumorigenic potential and inversely correlates with metastases in human cancers
Oncogene
35
4058-4068
2016
Homo sapiens
brenda
Brower, C.S.; Rosen, C.E.; Jones, R.H.; Wadas, B.C.; Piatkov, K.I.; Varshavsky, A.
Liat1, an arginyltransferase-binding protein whose evolution among primates involved changes in the numbers of its 10-residue repeats
Proc. Natl. Acad. Sci. USA
111
E4936-E4945
2014
Mus musculus
brenda
Jiang, Y.; Lee, J.; Lee, J.; Lee, J.; Kim, J.; Choi, W.; Yoo, Y.; Cha-Molstad, H.; Kim, B.; Kwon, Y.; Noh, S.; Kim, K.; Lee, M.
The arginylation branch of the N-end rule pathway positively regulates cellular autophagic flux and clearance of proteotoxic proteins
Autophagy
12
2197-2212
2016
Homo sapiens (O95260), Mus musculus (Q9Z2A5)
brenda
Kim, E.; Kim, S.; Lee, J.H.; Kwon, Y.T.; Lee, M.J.
Ablation of Arg-tRNA-protein transferases results in defective neural tube development
BMB Rep.
49
443-448
2016
Mus musculus (Q9Z2A5), Mus musculus 129SvEv/C57BL/6 (Q9Z2A5)
brenda
Kumar, A.; Birnbaum, M.; Patel, D.; Morgan, W.; Singh, J.; Barrientos, A.; Zhang, F.
Posttranslational arginylation enzyme Ate1 affects DNA mutagenesis by regulating stress response
Cell Death Dis.
7
e2378
2016
Homo sapiens (O95260), Homo sapiens, Mus musculus (Q9Z2A5), Mus musculus, Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Wang, J.; Pavlyk, I.; Vedula, P.; Sterling, S.; Leu, N.A.; Dong, D.W.; Kashina, A.
Arginyltransferase ATE1 is targeted to the neuronal growth cones and regulates neurite outgrowth during brain development
Dev. Biol.
430
41-51
2017
Mus musculus (Q9Z2A5), Mus musculus
brenda
Domitrovic, T.; Fausto, A.; Silva, T.; Romanel, E.; Vaslin, M.
Plant arginyltransferases (ATEs)
Genet. Mol. Biol.
40
253-260
2017
Arabidopsis thaliana (Q9ZT48), Chlamydomonas reinhardtii (A0A2K3D0B7), Oryza sativa Japonica Group (Q688J5), Physcomitrium patens (A0A2K1KVV8), Populus trichocarpa (A0A2K1YWL5), Sorghum bicolor (C5YYU0), Vitis vinifera (A0A438HA55)
brenda
Batsios, P.; Ishikawa-Ankerhold, H.C.; Roth, H.; Schleicher, M.; Wong, C.C.L.; Mueller-Taubenberger, A.
Ate1-mediated posttranslational arginylation affects substrate adhesion and cell migration in Dictyostelium discoideum
Mol. Biol. Cell
30
453-466
2019
Dictyostelium discoideum (Q55EI0), Dictyostelium discoideum, Dictyostelium discoideum AX2-214 (Q55EI0)
brenda
Hoernstein, S.N.; Mueller, S.J.; Fiedler, K.; Schuelke, M.; Vanselow, J.T.; Schuessele, C.; Lang, D.; Nitschke, R.; Igloi, G.L.; Schlosser, A.; Reski, R.
Identification of targets and interaction partners of arginyl-tRNA protein transferase in the moss Physcomitrella patens
Mol. Cell. Proteomics
15
1808-1822
2016
Physcomitrium patens (A0A2K1KVV8), Physcomitrium patens
brenda
White, M.D.; Klecker, M.; Hopkinson, R.J.; Weits, D.A.; Mueller, C.; Naumann, C.; O'Neill, R.; Wickens, J.; Yang, J.; Brooks-Bartlett, J.C.; Garman, E.F.; Grossmann, T.N.; Dissmeyer, N.; Flashman, E.
Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets
Nat. Commun.
8
14690
2017
Arabidopsis thaliana (Q9ZT48)
brenda
Singh, K.; Gupta, A.; Sarkar, A.; Gupta, I.; Rana, S.; Sarkar, S.; Khan, S.
Arginyltransferase knockdown attenuates cardiac hypertrophy and fibrosis through TAK1-JNK1/2 pathway
Sci. Rep.
10
598
2020
Rattus norvegicus
brenda
Wang, J.; Han, X.; Leu, N.A.; Sterling, S.; Kurosaka, S.; Fina, M.; Lee, V.M.; Dong, D.W.; Yates, J.R.; Kashina, A.
Protein arginylation targets alpha synuclein, facilitates normal brain health, and prevents neurodegeneration
Sci. Rep.
7
11323
2017
Mus musculus (Q9Z2A5), Mus musculus
brenda
Wang, J.; Pejaver, V.R.; Dann, G.P.; Wolf, M.Y.; Kellis, M.; Huang, Y.; Garcia, B.A.; Radivojac, P.; Kashina, A.
Target site specificity and in vivo complexity of the mammalian arginylome
Sci. Rep.
8
16177
2018
Mus musculus (Q9Z2A5), Mus musculus
brenda
Shim, S.M.; Choi, H.R.; Sung, K.W.; Lee, Y.J.; Kim, S.T.; Kim, D.; Mun, S.R.; Hwang, J.; Cha-Molstad, H.; Ciechanover, A.; Kim, B.Y.; Kwon, Y.T.
The endoplasmic reticulum-residing chaperone BiP is short-lived and metabolized through N-terminal arginylation
Sci. Signal.
11
eaan0630
2018
Homo sapiens (O95260)
brenda
Avcilar-Kucukgoze, I.; MacTaggart, B.; Kashina, A.
Functional interplay between arginyl-tRNA synthetases and arginyltransferase
Int. J. Mol. Sci.
23
10160
2022
Homo sapiens (O95260)
brenda
Kim, S.B.; Lee, J.S.; Lan, X.; Huang, W.; Taylor, D.J.; Kwon, Y.T.; Zhang, Y.; Ji, C.H.
The structure-function relationship of ATE1 R-transferase of the autophagic Arg/N-degron pathway
Autophagy
21
2293-2295
2025
Homo sapiens (O95260)
brenda
Cartwright, M.; Parakra, R.; Oduwole, A.; Zhang, F.; Deredge, D.J.; Smith, A.T.
Identification of an intrinsically disordered region (IDR) in arginyltransferase 1 (ATE1)
Biochemistry
63
3236-3249
2024
Mus musculus (Q9Z2A5)
brenda
Moorthy, B.T.; Jiang, C.; Patel, D.M.; Ban, Y.; OShea, C.R.; Kumar, A.; Yuan, T.; Birnbaum, M.D.; Gomes, A.V.; Chen, X.; Fontanesi, F.; Lampidis, T.J.; Barrientos, A.; Zhang, F.
The evolutionarily conserved arginyltransferase 1 mediates a pVHL-independent oxygen-sensing pathway in mammalian cells
Dev. Cell
57
654-669.e9
2022
Mus musculus (Q9Z2A5)
brenda
Jiang, C.; Moorthy, B.T.; Patel, D.M.; Kumar, A.; Morgan, W.M.; Alfonso, B.; Huang, J.; Lampidis, T.J.; Isom, D.G.; Barrientos, A.; Fontanesi, F.; Zhang, F.
Regulation of mitochondrial respiratory chain complex levels, organization, and function by arginyltransferase 1
Front. Cell Dev. Biol.
8
603688
2020
Mus musculus (Q9Z2A5)
brenda
Naga, R.; Poddar, S.; Bhattacharjee, A.; Kar, P.; Bose, A.; Mattaparthi, V.S.K.; Mukherjee, O.; Saha, S.
Structural analysis of human ATE1 isoforms and their interactions with Arg-tRNAArg
J. Biomol. Struct. Dyn.
42
7554-7573
2024
Homo sapiens (O95260)
brenda
Shokeen, K.; Baroi, M.K.; Chahar, M.; Das, D.; Saini, H.; Kumar, S.
Arginyltransferase 1 (ATE1)-mediated proteasomal degradation of viral haemagglutinin protein a unique host defence mechanism
J. Gen. Virol.
105
0000
2024
Gallus gallus
brenda
Van, V.; Ejimogu, N.E.; Bui, T.S.; Smith, A.T.
The Structure of Saccharomyces cerevisiae arginyltransferase 1 (ATE1)
J. Mol. Biol.
434
167816
2022
Saccharomyces cerevisiae (P16639), Saccharomyces cerevisiae ATCC 204508 (P16639)
brenda
Wang, J.; Kashina, A.S.
Assaying for arginyltransferase activity and specificity by peptide arrays
Methods Mol. Biol.
2620
123-127
2023
Homo sapiens (O95260)
brenda
Van, V.; Smith, A.T.
Reconstitution of the arginyltransferase (ATE1) iron-sulfur cluster
Methods Mol. Biol.
2620
209-217
2023
Mus musculus (Q9Z2A5), Saccharomyces cerevisiae
brenda
Wang, J.; Kashina, A.S.
Bacterial expression and purification of recombinant arginyltransferase (ATE1) and Arg-tRNA synthetase (RRS) for arginylation assays
Methods Mol. Biol.
2620
87-91
2023
Escherichia coli
brenda
Lan, X.; Huang, W.; Kim, S.B.; Fu, D.; Abeywansha, T.; Lou, J.; Balamurugan, U.; Kwon, Y.T.; Ji, C.H.; Taylor, D.J.; Zhang, Y.
Oligomerization and a distinct tRNA-binding loop are important regulators of human arginyl-transferase function
Nat. Commun.
15
6350
2024
Homo sapiens (O95260)
brenda
Fina, M.E.; Wang, J.; Nikonov, S.S.; Sterling, S.; Vardi, N.; Kashina, A.; Dong, D.W.
Arginyltransferase (Ate1) regulates the RGS7 protein level and the sensitivity of light-evoked ON-bipolar responses
Sci. Rep.
11
9376
2021
Mus musculus (Q9Z2A5)
brenda
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