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Literature summary for 2.3.2.8 extracted from

  • 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 (2016), Mol. Cell. Proteomics, 15, 1808-1822 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene PHYPA_004926, single copy gene, phylogenetic analysis Physcomitrium patens

Protein Variants

Protein Variants Comment Organism
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 Physcomitrium patens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arginyl-tRNAArg + protein Physcomitrium patens
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tRNAArg + L-arginyl-[protein]
-
?

Organism

Organism UniProt Comment Textmining
Physcomitrium patens A0A2K1KVV8
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-

Source Tissue

Source Tissue Comment Organism Textmining
gametophore young Physcomitrium patens
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meristem
-
Physcomitrium patens
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shoot
-
Physcomitrium patens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginyl-tRNAArg + protein
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Physcomitrium patens tRNAArg + L-arginyl-[protein]
-
?
additional information the enzyme interacts with sHSP17.2a, an Hsp20 class I chaperone Physcomitrium patens ?
-
-

Synonyms

Synonyms Comment Organism
arginyl-tRNA protein transferase
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Physcomitrium patens
ATE
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Physcomitrium patens

Expression

Organism Comment Expression
Physcomitrium patens 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 up

General Information

General Information Comment Organism
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 Physcomitrium patens
physiological function arginyltransferases (ATE) mediates N-terminal arginylation of secondary destabilizing residues (D, E, Cox) Physcomitrium patens