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Information on EC 4.6.1.19 - ribonuclease T2
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4.6.1.19 ribonuclease T2IUBMB Comments
A widely distributed family of related enzymes found in protozoans, plants, bacteria, animals and viruses that cleave ssRNA 3'-phosphate group with little base specificity. The enzyme catalyses a two-stage endonucleolytic cleavage. The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending with a 2',3'-cyclic phosphodiester, which are released from the enzyme. The enzyme then hydrolyses the cyclic products in a second reaction that takes place only when all the susceptible 3',5'-phosphodiester bonds have been cyclised. The second reaction is a reversal of the first reaction using the hydroxyl group of water instead of the 5'-hydroxyl group of ribose. The overall process is that of a phosphorus-oxygen lyase followed by hydrolysis to form the 3'-nucleotides.
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Word Map
- 4.6.1.19
- oligoadenylate
-
endoribonuclease
- 2',5'-oligoadenylate
- viruses
- dsrna
-
single-stranded
-
interferon-induced
-
2-5a-dependent
- s-rnases
-
ifn-induced
-
omega-3
- rhizopus
-
lauric
-
5'-phosphorylated
- polynucleotide
- niveus
- colicins
-
s-locus
-
interferon-regulated
- gametophytic
- rig-i
-
encephalomyocarditis
-
solanaceous
- oligoribonucleotides
-
ifn-beta
-
anticodons
-
dsrna-dependent
- pistil
-
self-compatible
-
xenotropic
- alata
-
ifn-stimulated
-
omega-hydroxylation
-
dsrna-activated
-
dinucleoside
- polyu
-
interferon-treated
- biotechnology
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
an [RNA fragment]-3'-nucleoside-3'-phosphate
+
a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
Synonyms
rnase l, omega-1, rnase t2, rnaset2, rnase i, acid rnase, ribonuclease l, rnase rh, acid ribonuclease, rnase m, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid ribonuclease
acid RNase
ACTIBIND
base non-specific ribonuclease
base nonspecific RNase
base-non-specific ribonuclease
EC 2.7.7.17
-
-
formerly
-
EC 3.1.27.1
-
-
formerly
-
EC 3.1.4.23
-
-
formerly
-
Escherichia coli ribonuclease I
-
-
-
-
non-base specific ribonuclease
nonbase-specific RNase
nonspecific RNase
nuclease, Escherichia coli ribo-, II
-
-
-
-
nuclease, ribo- (non-base specific)
-
-
-
-
ribonuclease
ribonuclease (non-base specific)
-
-
-
-
ribonuclease II
ribonuclease L
ribonuclease LE
ribonuclease M
ribonuclease MC1
ribonuclease N2
ribonuclease PP2
-
-
-
-
ribonuclease PP3
ribonuclease T2
ribonuclease U4
ribonucleate 3'-oligonucleotide hydrolase
-
-
-
-
ribonucleate nucleotido-2'-transferase (cyclizing)
-
-
-
-
RNAase CL
-
-
-
-
RNase
RNase (non-base specific)
RNase II
RNase Irp3
RNase L
RNase LE
RNase LX
RNase M
RNase MC
-
-
-
-
RNase MC1
RNase Ms
RNase T2
RNase X25
RNaseT2
S-like RNase
S1-RNase
-
-
-
-
S2-RNase
-
-
-
-
S3-RNase
-
-
-
-
S4-RNase
-
-
-
-
S5-RNase
-
-
-
-
S6-RNase
-
-
-
-
S7-RNase
-
-
-
-
T2 ribonuclease
T2 RNase
additional information
acid ribonuclease
-
-
-
-
acid RNase
-
-
-
-
base-non-specific ribonuclease
-
-
-
-
non-base specific ribonuclease
-
-
-
-
nonbase-specific RNase
-
-
-
-
nonspecific RNase
-
-
-
-
ribonuclease II
-
-
-
-
ribonuclease M
-
-
-
-
ribonuclease N2
-
-
-
-
ribonuclease PP3
-
-
-
-
ribonuclease U4
-
-
-
-
RNase (non-base specific)
-
-
-
-
RNase II
-
-
-
-
RNase LE
-
-
-
-
RNase LX
-
-
-
-
RNase M
-
-
-
-
RNase Ms
-
-
-
-
RNase T2
-
-
-
-
additional information
-
the enzyme is a conserved member of the RNase T2 family
additional information
-
the enzyme belongs to the RNaseT2 enzyme family
additional information
-
the enzyme belongs to the RNaseT2 enzyme family
additional information
-
the enzyme belongs to the RNaseT2 enzyme family
additional information
-
enzymes belong to the RNase 1-type and are S-like RNases
additional information
the enzyme is a class II enzyme of the RNase T2 family
additional information
enzyme belongs to the ribonuclease T2 family, structure comparison and amino acid sequence alignment
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an [RNA fragment]-3'-nucleoside-2',3'-cyclophosphate + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate
(1b)
-
-
-
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
RNA = an [RNA fragment]-3'-nucleoside-2',3'-cyclophosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
(1a)
-
-
-
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
mechanism
-
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
reaction mechanism
-
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
reaction mechanism
-
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
similar enzyme with possilbly exonucleolytic mechanism
-
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
two-stage endonucleolytic cleavage to 3'-phosphomononucleotides and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates: first step reversible cleavage of phosphodiester bond between 3'-adenylic acid group and 5'-hydroxyl group at adjacent nucleotides in RNA chain with formation of nucleoside 2',3'-cyclic phosphates and oligonucleotides with 2',3'-cyclic phosphate at 3'-terminal, second step: hydrolysis of terminal cyclic phosphate groups with formation of corresponding 3'-phosphates
-
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
active site structure, Glu32 is an essential part of the B2-substrate recognition and binding site
-
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
catalytic hydrolysis mechanism, active site structure, the conserved active site residues His39, His92, and His 97 are essential for activity, Glu93 and Lys96 are important
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
Phe101 is important for catalytic activity
-
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
reaction mechanism, His109, Lys108, His104, and His46 are involved
-
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
residues His34, His 83, Glu84, Lys87, and His88 may be involved in catalysis
-
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
substrate recognition, binding and specificity, Asn71 and Leu73 are involved
-
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
overall reaction
-
-
-
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
mechanism of RNA recognition, binding and cleavage by RNase L, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
[RNA] 5'-hydroxy-ribonucleotide-3'-[RNA fragment]-lyase (cyclicizing; [RNA fragment]-3'- nucleoside-2',3'-cyclophosphate-forming and hydrolysing)
A widely distributed family of related enzymes found in protozoans, plants, bacteria, animals and viruses that cleave ssRNA 3'-phosphate group with little base specificity. The enzyme catalyses a two-stage endonucleolytic cleavage. The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending with a 2',3'-cyclic phosphodiester, which are released from the enzyme. The enzyme then hydrolyses the cyclic products in a second reaction that takes place only when all the susceptible 3',5'-phosphodiester bonds have been cyclised. The second reaction is a reversal of the first reaction using the hydroxyl group of water instead of the 5'-hydroxyl group of ribose. The overall process is that of a phosphorus-oxygen lyase followed by hydrolysis to form the 3'-nucleotides.
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CAS REGISTRY NUMBER
COMMENTARY
37278-25-4
-
9075-06-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2',3'-cyclic NMP + H2O
3'(2')-NMP
-
slower side reaction, intrinsic cyclic nucleotide phosphodiesterase activity
-
-
?
nucleotidyl-3',5'-nuceotide + H2O
2',3'-cyclic NMP + 3'(2')-NMP
-
determination of base specificity
-
-
?
RNA
?
-
acetate buffer pH 5.0 or Tris-HCl pH 7.5, 37 °C, 5 min incubation
-
-
?
RNA + H2O
2',3'-cyclic NMP + 3'(2')-NMP
-
high-molecular weight fraction of RNA from Torula yeast, typeII-S
2',3'-cyclic NMPs are are further hydrolyzed in a side reaction
-
?
poly-8 adenylic acid
AMP + ?
-
pH 8, 1 mM MgCl2, incubation at 30°C for 5 min
-
-
?
poly-8 adenylic acid
AMP + ?
-
pH 8, 1 mM MgCl2, incubation at 30°C for 5 min
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
two-stage endonucleolytic cleavage to 3'-phosphomononucleotides and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates, first step reversible cleavage of phosphodiester bond between 3'-adenylic acid group and 5'-hydroxyl group at adjacent nucleotides in RNA chain with formation of nucleoside 2',3'-cyclic phosphates and oligonucleotides with 2',3'-cyclic phosphate at 3'-terminal, second step: hydrolysis of terminal cyclic phosphate groups with formation of corresponding 3'-phosphates, no base specificity
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
preference for adenylic acid linkages in RNA
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
rates of release of 2',3'-cyclic nucleotides in decreasing order: guanylic acid, adenylic acid, cytidylic acid, uridylic acid
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
release rates in decreasing order: GMP, UMP, AMP, CMP
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
hydrolyzes in 3'- to 5'-direction, hydrolyzes single stranded RNA
-
?
RNA + H2O
3'-phosphomononucleotides
-
2',3'-cyclic nucleotide intermediates
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
release rates in order 3'-UMP, 3'-GMP, 3'-AMP
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
poly(A), poly(I), poly(C), poly(U)
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
polyguanylic acid and duplexes of synthetic homopolymers less sensitive
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
preference for pC-purine bonds
-
-
?
RNA + H2O
?
-
RNase L cleaves RNAs predominantly after single-stranded UA and UU dinucleotides
-
-
?
RNA + H2O
nucleoside 3'-phosphates + 3'-phosphooligonucleotides
-
5S rRNA and tRNA from Escherichia coli
-
-
?
RNA + H2O
nucleoside 3'-phosphates + 3'-phosphooligonucleotides
-
5S rRNA and tRNA from Escherichia coli
-
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
from yeast
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
squid
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
additional information
?
-
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
?
additional information
?
-
-
the enzyme ACTIBIND is able to bind actin in vitro
-
-
?
additional information
?
-
-
transphosphorylation of adenylyl (3'-5') uridine and adenosine 3'-(1-naphthylphosphate)
-
-
?
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
?
additional information
?
-
-
RNase degrades uracil containing nucleic acids only
-
-
?
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
?
additional information
?
-
-
assay substrate is Torula yeast RNA
-
-
?
additional information
?
-
-
assay substrate is Torula yeast RNA
-
-
?
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
?
additional information
?
-
-
the enzyme ceases degradation when it approaches a double stranded region, the enzyme also cannot digest stable, helical regions of RNA
-
-
?
additional information
?
-
-
tRNAs that contains the hypermodified nucleoside queuosine, Q, at the wobble position
-
-
?
additional information
?
-
-
two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
-
-
?
additional information
?
-
-
enzyme concentration in plasma is increased in case of impaired glomerular filtration rate of the kidney, patients suffering chronic renal insufficiency accumulate the enzyme in the plasma low molecular weight fraction
-
-
?
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
?
additional information
?
-
cleavage of biological targets by the enzyme with site selection in mammalian ribosomes and hepatitis C virus RNA, overview
-
-
?
additional information
?
-
-
cleavage of biological targets by the enzyme with site selection in mammalian ribosomes and hepatitis C virus RNA, overview
-
-
?
additional information
?
-
-
RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides
-
-
?
additional information
?
-
-
the enzyme cleaves single-stranded RNA molecules
-
-
?
additional information
?
-
-
the enzyme is active on rRNA, rRNA cleavage products are generated from intact ribosomes in ovarian cancer Hey1b cells
-
-
?
additional information
?
-
-
assay substrate is 32P-labeled synthetic substrate r(C11U2C7)
-
-
?
additional information
?
-
the enzyme cleaves 3' of UN sequences, RNA sequence recognition involves the KEN domain homodimer, RNA cleavage is carried out by the symmetry-related histidine H672 provided by homodimerization, a single H672 residue per a KEN/KEN dimer is necessary and sufficient for RNA cleavage, overview. With Angptl3 mRNA as substrate, RIDD cleavage sites and the consensus UN-N are utilized by RNase L, Cyp1 mRNAs and pre-mir-17microRNA are all cleaved at UG-C sites
-
-
?
additional information
?
-
-
the enzyme cleaves 3' of UN sequences, RNA sequence recognition involves the KEN domain homodimer, RNA cleavage is carried out by the symmetry-related histidine H672 provided by homodimerization, a single H672 residue per a KEN/KEN dimer is necessary and sufficient for RNA cleavage, overview. With Angptl3 mRNA as substrate, RIDD cleavage sites and the consensus UN-N are utilized by RNase L, Cyp1 mRNAs and pre-mir-17microRNA are all cleaved at UG-C sites
-
-
?
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
?
additional information
?
-
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
?
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
?
additional information
?
-
-
enzyme preferentially cleaves the 5'-side of uridine, Asn71 and Leu73 are involved in substrate specificity
-
-
?
additional information
?
-
-
the enzyme serves as a self-incompatibility factor, a mechanism that prevents pollen from one flower from fertilizing other flowers of the same plant
-
-
?
additional information
?
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
?
additional information
?
-
-
induced upon tobacco mosaic virus infection, structure determined, substrate-binding sites studied with nucleoside monophosphates at concentrations between 1 and 10 mM followed by crystallization
-
-
?
additional information
?
-
-
the enzyme confers hypersensitive response and aquired resistance to pathogens
-
-
?
additional information
?
-
-
RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides
-
-
?
additional information
?
-
-
subsite base specificities at the B1 and B2 site of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
subsite base specificities at the B1 and B2 site of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
?
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
?
additional information
?
-
-
besides other physiological functions in leaf and flower senescence and response to plant hormones, phosphate starvation, and wounding, the enzymes play a role in self-incompatibility cell-to-cell interactions
-
-
?
additional information
?
-
-
RNase LX is related to RNA metabolism in the final stage of senescence, all enzyme forms are related in phosphate remobilization
-
-
?
additional information
?
-
-
enzymes show preference for release of guanine mononucleotides from diribonucleoside monophosphates or RNA, preference in descending order is G, A, U, C
-
-
?
additional information
?
-
induced expression upon phosphate-starvation, tissue-specific expression patterns in roots analyzed, role during the phosphate starvation response suggested
-
-
?
additional information
?
-
-
induced expression upon phosphate-starvation, tissue-specific expression patterns in roots analyzed, role during the phosphate starvation response suggested
-
-
?
additional information
?
-
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
RNA + H2O
?
-
RNase L cleaves RNAs predominantly after single-stranded UA and UU dinucleotides
-
-
?
additional information
?
-
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
?
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
?
additional information
?
-
-
RNase degrades uracil containing nucleic acids only
-
-
?
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
?
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
?
additional information
?
-
-
tRNAs that contains the hypermodified nucleoside queuosine, Q, at the wobble position
-
-
?
additional information
?
-
-
two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
-
-
?
additional information
?
-
-
enzyme concentration in plasma is increased in case of impaired glomerular filtration rate of the kidney, patients suffering chronic renal insufficiency accumulate the enzyme in the plasma low molecular weight fraction
-
-
?
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
?
additional information
?
-
cleavage of biological targets by the enzyme with site selection in mammalian ribosomes and hepatitis C virus RNA, overview
-
-
?
additional information
?
-
-
cleavage of biological targets by the enzyme with site selection in mammalian ribosomes and hepatitis C virus RNA, overview
-
-
?
additional information
?
-
-
RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides
-
-
?
additional information
?
-
-
the enzyme cleaves single-stranded RNA molecules
-
-
?
additional information
?
-
-
the enzyme is active on rRNA, rRNA cleavage products are generated from intact ribosomes in ovarian cancer Hey1b cells
-
-
?
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
?
additional information
?
-
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
?
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
?
additional information
?
-
-
the enzyme serves as a self-incompatibility factor, a mechanism that prevents pollen from one flower from fertilizing other flowers of the same plant
-
-
?
additional information
?
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
?
additional information
?
-
-
the enzyme confers hypersensitive response and aquired resistance to pathogens
-
-
?
additional information
?
-
-
RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides
-
-
?
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
?
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
?
additional information
?
-
-
besides other physiological functions in leaf and flower senescence and response to plant hormones, phosphate starvation, and wounding, the enzymes play a role in self-incompatibility cell-to-cell interactions
-
-
?
additional information
?
-
-
RNase LX is related to RNA metabolism in the final stage of senescence, all enzyme forms are related in phosphate remobilization
-
-
?
additional information
?
-
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
additional information
-
Mg2+ and ATP or ADP protect the enzyme from proteolytic cleavage
additional information
no significant inhibitory effect of cobalt, nickel or magnesium at 50 mM concentration
additional information
-
no significant inhibitory effect of cobalt, nickel or magnesium at 50 mM concentration
additional information
-
RNases LE, LX and LV-3 do not require divalent cations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
protein Im5
-
immunity protein, in the study different mutants of Im5 are investigated
-
diethyl dicarbonate
-
above pH 6.0, no inactivation in presence of 3'-AMP
iodoacetamide
-
irreversible inhibition at pH 5.0, modification site is one of the two catalytic His residues
iodoacetamide
-
irreversible inhibition at pH 5.0, modification site is one of the two catalytic His residues
iodoacetamide
-
irreversible inhibition at pH 5.0, modification site is one of the two catalytic His residues
iodoacetate
-
irreversible inhibition at pH 5.0, modification site is one of the two catalytic His residues
iodoacetate
-
irreversible inhibition at pH 5.0, modification site is one of the two catalytic His residues
iodoacetate
-
irreversible inhibition at pH 5.0, modification site is one of the two catalytic His residues
additional information
-
inhibitory effect of mononucleotide phosphates in descending order 2'-AMP, 2'-GMP, 3'-AMP, 2'-CMP, 2'(3')-UMP
-
additional information
-
inhibitory effect of mononucleotide phosphates in descending order 2'-AMP, 2'-GMP, 3'-AMP, 2'-CMP, 2'(3')-UMP
-
additional information
-
inhibitory effect of mononucleotide phosphates in descending order 2'-AMP, 2'-GMP, 3'-AMP, 2'-CMP, 2'(3')-UMP
-
additional information
-
no effect of 2.5 mM EDTA, no product inhibition
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2',5'-linked oligoadenylates
two different binding sites in the enzyme's ANK domain and a third site in the N lobe of the KH domain, sensing mechanism, structure-function analysis, overview. The KH/KH and kinase extension nuclease (KEN)/KEN interfaces are important in 2',5'-oligoadenylate-dependent enzyme activation
-
2'-5'-linked oligoadenylates
-
natural 2'-5'-linked tetraadenylates and three tetramers with 3'-end AMP units replaced with ribo-, arabino- and xylo-configured phosphonate analogues of AMP are enzyme activators with equal potency. The enzyme is activated by the binding of 2'-5'-linked oligoadenylates to the N-terminal ankyrin repeat domain, which causes the inactive monomer to form a catalytically active homodimer
-
2'-5'-oligoadenylate
-
short polyadenylate molecules that are connected by unique 2'-5' linkages, collectively referred to as 2-5A. 2-5A induces dimerization via the ANK domain and this dimerization correlates with activation of ribonuclease activity
citrate
-
25 mM sodium citrate buffer results in 170% activity compared to 100% activity in sodium acetate buffer, both pH 5.6
phosphate
-
25 mM sodium phosphate buffer results in 153% activity compared to 100% activity in sodium acetate buffer, both pH 5.6
viral dsRNA
-
viral dsRNA provokes the synthesis of 2'-5' oligoadenylate, 2-5A, binding of 2-5A to ankyrin repeats of monomeric RNase L leads to RNase L dimerization and activation
-
2',5'-Oligoadenylate
-
mediates the enzyme activity, absolutely required for activity
2',5'-Oligoadenylate
-
the enzyme's pseudokinase domain is involved in the natural activator sensing, binding site and structure, modeling, overview. Quantitative determination of specific binding of the full-length enzyme and of isolated enzyme ANK domain to immobilized biotinylated 2',5'-oligoadenylate
2',5'-Oligoadenylate
-
binds to and activates the enzyme. It is produced in response to viral double-stranded RNA by the 2',5'-oligoadenylate synthetase
2',5'-Oligoadenylate
-
the enzyme's pseudokinase domain is involved in the natural activator sensing, binding site and structure, modeling, overview. Quantitative determination of specific binding of the full-length enzyme and of isolated enzyme ANK domain to immobilized biotinylated 2',5'-oligoadenylate
additional information
-
EDTA activates soluble enzyme, no effect on immobilized
-
additional information
-
a dephosphorylated form of 2',5'-oligoadenylate does not activate RNase L
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH-dependence of Km, 2 kinetically distinct forms
-
additional information
additional information
-
RNA: 555 mg/ml soluble enzyme, 266 mg/ml immobilized enzyme
-
additional information
additional information
-
Km values for mutant enzymes with diverse dinucleotide substrates, overview
-
additional information
additional information
-
Km values for mutant enzymes with diverse dinucleotide substrates, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH-dependence of turnover-number, 2 kinetically distinct forms
-
additional information
additional information
-
wild-type and mutant enzymes
-
additional information
additional information
-
consists of seven helices and seven beta strands, determined by crystallization
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1600
additional information
additional information
-
enzyme levels at different kidney glomerular filtration rates of blood
additional information
determined by total RNase activity and in-gel activity assay
additional information
-
determined by total RNase activity and in-gel activity assay
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
5.5
5.8
6 - 6.3
-
hydrolysis of various nucleoside 2',3'-cyclic phosphates, degradation of 3'-nucleotide benzyl ester
6.5
7.4
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 5.5
-
pH 3.5, 5.5: about 70% of activity maximum, soluble and immobilized enzyme
3.5 - 6
-
pH 3.5: 80% of activity maximum, soluble and immobilized form, pH 6: soluble form 100%, immobilized form 90% of maximum acitivity
3.5 - 6.5
-
pH 3.5: about 20% of activity maximum, 6.5: less than 10% of activity maximum
additional information
additional information
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
additional information
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
additional information
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
additional information
-
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 70
40 - 70
-
40°C: about 60% of activity maximum, soluble and immobilized enzyme, 70°C: about 70% immobilized enzyme, 40% soluble enzyme, of activity maximum
40 - 70
-
40°C: 100% activity of immobilized enzyme, 70°C: 20% of maximum activity of immobilized enzyme
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
multiple forms: RNase T2, RNase T2-L1-5, common protein moiety, heterogeneities due to carbohydrate content
-
-
brenda
rnalx gene, intracellular ribonuclease LX precursor; cv. Lukullus
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
RNaseLE transcript accumulation occurs preferentially upon wounding
brenda
additional information
-
Takadiastase powder
brenda
the CP1412 protein is exclusively secreted/excreted from eggs, but not cercariae and adult worms
brenda
-
transfected with pcDNA3 vectors to establish a cell line overexpressing wild-type RNase L, with a dominant negative mutation, and control HeLa cells carrying the vector alone
brenda
-
e.g. ATCC CCL-2 and S3, express normal enzyme level, while strain HeLa-M is defective in RNase L expression
brenda
neuroendocrine neoplasms of the lung, well differentiated and poorly differentiated
brenda
meristematic zone at root tip and elongation zone at root tip
brenda
additional information
-
the enzyme is the main endoribonuclease activity in plant cells
brenda
additional information
-
rnaset2 is expressed ubiquitously in zebrafish embryos and adults from conception
brenda
additional information
-
developmental profile of Drosophila melanogaster enzyme activities, overview
brenda
additional information
-
developmental profile of Drosophila melanogaster enzyme activities, overview
-
brenda
additional information
-
RNase L mRNA is constitutively and differentially expressed in nine different mouse tissues, its level is maximal in immunological tissues (spleen, thymus and lungs), moderate in reproductive tissues (testis and prostate), and low in metabolic tissues (kidney, brain, liver and heart), semi-quantitative RT-PCR expression analysis, overview
brenda
additional information
-
during a human infection this worm lays its eggs in its definitive mammalian host, and these eggs secrete a factor termed omega-1, which is a known RNaseT2 family member
brenda
additional information
low RNaseLER transcript abundances in almost all parts of tomato plants
brenda
additional information
-
low RNaseLER transcript abundances in almost all parts of tomato plants
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme Rny1p requires entering into the endoplasmic reticulum first to become active by N-glycosylation and uses the adaptor protein Erv29p for packaging into COPII vesicles and transport to the Golgi apparatus, which results in the further attachment of high-glycans. Whereas modifications with glycans are dispensable for the nucleolytic activity of Rny1p, Golgi-mediated modifications are critical for its extracellular secretion. Function of Golgi glycosylation in a T2 RNase as a sorting and secretion signal
brenda
epidermal cells of lateral and adventitious root primordia
brenda
-
RNase T2 is located within a region of the long arm of chromosome six that undergoes deletion or rearrangement in many cancers, including some cases of adult T-cell leukemia, ATL
brenda
additional information
-
molecular mechanisms controlling intra- and extracellular localization of enzyme Rny1p , overview. Failure of Golgi-specific glycosylation appears to direct the enzyme to the vacuole as an alternative destination and/or site of terminal degradation, the unglycosylated mutants are unable to be secreted
-
brenda
-
and derived structures, e.g. endoplasmic reticulum-derived bodies
brenda
-
the 18 N-terminal amino acids form the signal peptide responsible for enzyme entry into the endoplasmic reticulum lumen. Enzyme Rny1p requires entering into the endoplasmic reticulum first to become active by N-glycosylation and uses the adaptor protein Erv29p for packaging into COPII vesicles and transport to the Golgi apparatus, wich results in the further attachment of high-glycans
brenda
-
whereas modifications with glycans are dispensable for the nucleolytic activity of Rny1p, Golgi-mediated modifications are critical for its extracellular secretion
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
RNS2 is part of a process that degrades rRNA to recycle its components and is conserved in all eukaryotes
evolution
-
involvement of the pseudokinase domain of the enzyme cofactor sensing, nucleotide binding, dimerization, and ribonuclease functions highlights the evolutionary adaptability of the eukaryotic protein kinase fold
evolution
-
involvement of the pseudokinase domain of the enzyme cofactor sensing, nucleotide binding, dimerization, and ribonuclease functions highlights the evolutionary adaptability of the eukaryotic protein kinase fold
evolution
-
RNase T2 family, phylogenetic analysis, gene duplication events seem to have happened independently in each phylum. RNase T2 genes have undergone duplication events followed by divergence in several phyla, including the loss of catalytic residues, and suggest that RNase T2 proteins have acquired additional functions. Among those, it is likely that a role in host immunosuppression evolved independently in several groups, including parasitic Platyhelminthes and parasitoid wasps
evolution
RNase T2 is the only member of the Rh/T2/S family of acidic hydrolases in humans, its structure shows a typical fold for members of the T2 RNase family with seven alpha-helices and eight beta-strands constituting an alpha+beta motif, as most of the central anti-parallel beta-sheet is clearly separated in the sequence from the helical parts. The alpha + beta core fold shows high similarity to those of known T2 RNase structures from plants, while, in contrast, the external loop regions show distinct structural differences
evolution
-
RNase X25 belongs to the RNase T2 family which harbors enzymes associated with the secretory pathway that are almost absolutely conserved in all eukaryote
evolution
-
RNase X25 belongs to the RNase T2 family which harbors enzymes associated with the secretory pathway that are almost absolutely conserved in all eukaryote
-
malfunction
-
loss of rnaset2 in mutant zebrafish results in accumulation of undigested rRNA within lysosomes within neurons of the brain, the mutants show white matter lesions correlating with accumulation of amyloid precursor protein and astrocytes at sites of neurodegeneration
malfunction
-
mutants lacking RNS2 activity accumulate RNA intracellularly, and rRNA in these mutants has a longer half-life, rns2 mutants display constitutive autophagy, phenotypes, overview
malfunction
-
RNaseT2 family members are implicated in human pathologies such as cancer and parasitic diseases. Humans lacking RNASET2 manifest a defect in neurological development, perhaps due to aberrant control of the immune system. Mutations in RNASET2 are identified as the causative lesion in an autosomal recessive disorder leading to cystic leukoencephalopathy, overview
malfunction
-
disruption of the RNase T2 family gene limits the organism's ability to colonize polystyrene, polypropylene, glass, and stainless steel surfaces, transposon mutagenesis analysis of abiotic surface-colonization of wild-type and mutant strain 98-37-09, the mutant exhibits reduced expression of 29 genes, 15 of which are predicted to be associated with bacterial attachment and surface-associated motility, overview
malfunction
-
GFP-tagged enzyme wild-type and mutants N37Q/N70Q/N103Q/N123Q and W399R localize to the vacuole, the unglycosylated mutants are unable to be secreted, overview. Glycosylation-defective Rny1p mutants are not destroyed via the ERAD mechanism
malfunction
mutations in the gene of human enzyme RNase T2 are associated with white matter disease of the human brain showing bilateral temporal lobe cysts and multifocal white matter lesions which lead to psychomotor impairments,spasticity and epilepsy
malfunction
-
siRNA-mediated depletion of endogenous enzyme in the human ovarian cancer cell line Hey1b increased the levels of LINE-1 retrotransposition by about 2fold. Recombinant expression of wild-type and a constitutively active deletion mutant enzyme form, but not a catalytically inactive enzyme mutant R667A, impair the mobility of engineered human LINE-1 and mouse intracisternal A-type particle retrotransposons in cultured human cells
malfunction
-
virus-mediated autophagy is deficient in cells lacking RNase L, overview
malfunction
depletion of CP1412 from soluble egg antigen impairs the ability of soluble egg antigen to induce M2 type polarization of RAW264.7macrophages. Immunizing mice with CP1412 induces high antibody titers, increased serum IL-4 and TGF-beta levels and splenic CD4 + CD25 + Foxp3 + T cells, downregulated serum IFN-gamma levels and alleviated the egg granuloma pathology of schistosome infection. In vitro stimulation by rSj CP1412 significantly increased CD4 + CD25 + Foxp3 + T cell numbers in splenocytes of healthy mice. The CP1412 protein with RNase activity inactivated by diethyldicarbonate fails to induce M2 surface marker CD206 expression in RAW264.7 macrophages
malfunction
knockdown of the protein in an immortalized mouse cell line TM6 decreases the degradation rate
malfunction
-
disruption of the RNase T2 family gene limits the organism's ability to colonize polystyrene, polypropylene, glass, and stainless steel surfaces, transposon mutagenesis analysis of abiotic surface-colonization of wild-type and mutant strain 98-37-09, the mutant exhibits reduced expression of 29 genes, 15 of which are predicted to be associated with bacterial attachment and surface-associated motility, overview
-
metabolism
-
cellular functions of RNase T2 proteins are associated with RNA recycling and maintenance of cellular homeostasis
metabolism
-
the interferon-inducible antiviral state is mediated in part by the 2',5'-oligoadenylate synthetase/RNase L system
metabolism
modulates inflammasome-dependent IL-1beta secretion in macrophages
metabolism
stimulating RAW264.7 macrophages with recombinant CP1412 raises the expression of CD206, Arg-1 and IL-10, which are related to M2 type macrophage differentiation. Stimulating dendritic cells with rSjCP1412 fails to induce their maturation, and the recombinant protein also inhibits LPS-stimulated dendritic cell maturation
metabolism
the enzyme degrades mitochondrial RNAs and it is also responsible for selective degradation of the cytosolic rRNAs on the outer membrane. The degradation activity also has a positive effect on nuclear transcription of rRNAs, suggesting a compensatory feedback mechanism, and affects protein translations in and out of mitochondria
metabolism
the enzyme degrades mitochondrial RNAs and it is also responsible for selective degradation of the cytosolic rRNAs on the outer membrane. The degradation activity also has a positive effect on nuclear transcription of rRNAs, suggesting a compensatory feedback mechanism, and affects protein translations in and out of mitochondria
metabolism
there is a possible link between the hypoxic state experienced by cancer cells and the expression level of RNASET2. A role of this gene as a stress-response factor is postulated
metabolism
-
cellular functions of RNase T2 proteins are associated with RNA recycling and maintenance of cellular homeostasis
-
physiological function
the zebrafish genome contains two RNase T2 genes, RNase Dre1 and RNase Dre2. These genes are part of two phylogenetic clades, one conserved in all chordates (the RNase Dre2 clade), and another fish-specific (the RNase Dre1 clade). RNase T2 enzymes carry out a housekeeping function
physiological function
-
ACTIBIND inhibits the clonogenicity and invasiveness of various tumors in culture and in mouse models. ACTIBIND disrupts the fine actin networks at the interior of colon cancer cells. Interaction of RNaseT2 proteins with the actin cytoskeleton provides a possible mechanism for RNase-independent cytotoxicity
physiological function
-
ribonuclease T2 is known to play a role in senescence in plants and possibly mammalian cells and may be an important tumor suppressor
physiological function
RNaseLER represents a constitutively expressed gene with a cell-specific role in stomata and trichomes and no involvement in stress responses
physiological function
-
RNaseT2 omega-1 is the major component in priming dendritic cells for Th2 polarization of CD4+ T cells during infection, a process depending on the RNase activity of omega-1
physiological function
-
RNaseT2 protein secreted by the purine auxotroph Entamoeba histolytica might function in scavenging purines from this amoeba's host
physiological function
-
RNS2, an intracellular RNase T2 from Arabidopsis thaliana, is essential for normal ribosomal RNA recycling. RNS2 is part of a process that degrades rRNA to recycle its components
physiological function
-
the envelope glycoprotein, termed Erns, has an RNaseT2 domain and ribonuclease activity, and is secreted by infected cells, the RNaseT2 protein induces cytotoxicity against host lymphocytes, but not epithelial cells, of various host species, and modulates host immune cell function
physiological function
-
the envelope glycoprotein, termed Erns, has an RNaseT2 domain and ribonuclease activity, and is secreted by infected cells, the RNaseT2 protein induces cytotoxicity against host lymphocytes, but not epithelial cells, of various host species, and modulates host immune cell function
physiological function
-
direct activation of the enzyme by transfection with 2',5'-oligoadenylate induces IFN-beta in embryonic fibroblasts but not in macrophages, RNA damage from the enzyme in virus-infected macrophages is likely responsible for reducing IFN-beta production. Apoptosis is known to occur in cells that sustain high levels of RNA damage due to RNase L enzyme activity
physiological function
-
interferon-inducible 2',5'-oligoadenylate-dependent ribonuclease L is a uniquely regulated endoribonuclease, a key player in the innate antiviral immune defense mechanismsof mammalian cells induced by interferons. The enzyme might have more general cellular functions through protein-protein interactions in the spleen for immune response in mammals. Cellular enzyme-interacting proteins from spleen are fibronectin precursor, beta-actin, troponin I, myosin heavy chain 9 (non-muscle), growth-arrest specific protein 11, clathrin light chain B, a putative uncharacterized protein (Ricken cDNA 8030451F13) isoform (CRA d) and alanyl tRNA synthetase
physiological function
-
RNase L is an ankyrin repeat domain-containing dual endoribonuclease-pseudokinase that is activated by unusual 2',5'-oligoadenylate second messengers and impedes viral infections in higher vertebrates. The enzyme is important in interferon-regulated antiviral innate immunity. Molecular basis for the regulation of the enzyme's antiviral function, overview
physiological function
-
RNase L is an ankyrin repeat domain-containing dual endoribonuclease-pseudokinase that is activated by unusual 2',5'-oligoadenylate second messengers and impedes viral infections in higher vertebrates. The enzyme is important in interferon-regulated antiviral innate immunity. Molecular basis for the regulation of the enzyme's antiviral function, overview
physiological function
-
RNase X25 enzyme has a housekeeping role in recycling RNA and in stress responses, it is the major contributor of ribonuclease activity in flies, correlation between induction of RNase X25 expression and autophagy
physiological function
-
RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides and also possess antitumorigenic and antiangiogenic activities. The enzyme binds actin and interferes with the cytoskeletal network structure, thereby inhibiting cell motility and invasiveness in cancer and in endothelial cells. Two structural elements create the binding site for actin, that is composed of one cysteine residue and one conserved amino acid region. The actin binding sites possibly interfere with the cytoskeleton network structure and as such may be responsible for the antitumorigenic and antiangiogenic activities of the enzyme
physiological function
-
RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides and also possess antitumorigenic and antiangiogenic activities. The enzyme binds actin and interferes with the cytoskeletal network structure, thereby inhibiting cell motility and invasiveness in cancer and in endothelial cells. Two structural elements create the binding site for actin, that is composed of one cysteine residue and one conserved amino acid region. The actin binding sites possibly interfere with the cytoskeleton network structure and as such may be responsible for the antitumorigenic and antiangiogenic activities of the enzyme. The enzyme inhibits human umbilical vein endothelial cell tube formation
physiological function
-
the 2',5'-oligoadenylate/RNase L system is a RNA virus-activated host RNase pathway that disposes of or processes viral and cellular single-stranded RNAs. Activation of RNase L during viral infections induces autophagy, autophagy induction by RNase L modulates viral growth
physiological function
-
the enzyme is a positive regulator of Acinetobacter baumannii's ability to colonize inanimate surfaces and motility
physiological function
-
the enzyme might function as a suppressor of structurally distinct retrotransposons, endogenous RNase L restricts L1 retrotransposition, overview. Wild-type enzyme, but not enzyme mutant R667A, prevents formation of LINE-1 cytoplasmic foci
physiological function
-
the ribonuclease RNase L is activated by the binding to 2'-5'-oligoadenylates and it proceeds to cleave single-stranded RNA molecules, ultimately leading to apoptosis of the virally infected cell
physiological function
-
interferon-inducible 2',5'-oligoadenylate-dependent ribonuclease L is a uniquely regulated endoribonuclease, a key player in the innate antiviral immune defense mechanismsof mammalian cells induced by interferons. The enzyme might have more general cellular functions through protein-protein interactions in the spleen for immune response in mammals. Cellular enzyme-interacting proteins from spleen are fibronectin precursor, beta-actin, troponin I, myosin heavy chain 9 (non-muscle), growth-arrest specific protein 11, clathrin light chain B, a putative uncharacterized protein (Ricken cDNA 8030451F13) isoform (CRA d) and alanyl tRNA synthetase
-
physiological function
-
RNase X25 enzyme has a housekeeping role in recycling RNA and in stress responses, it is the major contributor of ribonuclease activity in flies, correlation between induction of RNase X25 expression and autophagy
-
physiological function
-
the enzyme is a positive regulator of Acinetobacter baumannii's ability to colonize inanimate surfaces and motility
-
additional information
-
a reduction in the level of RNase T2 by Tax may play a role in adult T-cell leukemia, ATL, development, one of the primary diseases caused by human T cell leukemia virus type 1, HTLV-1, infection, ability of the viral protein to directly deregulate expression of specific cellular genes through interactions with numerous transcriptional regulators, e.g. the virally-encoded Tax protein, overview. Tax is renriched at the RNASET2 gene
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
enzyme mode of action independent of its enzymatic activity, overview. The enzyme has four disulfide bridges, connecting cysteine residues 48/55, 75/121, 184/241 and 202/213, its catalytic site comprises residues His65, His113, Glu114, Lys117 and His118
additional information
-
enzyme mode of action independent of its enzymatic activity, overview. The enzyme has four disulfide bridges, connecting cysteine residues 48/55, 75/121, 184/241 and 202/213, its catalytic site comprises residues His65, His113, Glu114, Lys117 and His118
additional information
-
enzyme Rny1p requires entering into the endoplasmic reticulum first to become active and uses the adaptor protein Erv29p for packaging into COPII vesicles and transport to the Golgi apparatus
additional information
-
involvement of the pseudokinase domain of the enzyme activator sensing, nucleotide binding, dimerization, and ribonuclease functions
additional information
-
involvement of the pseudokinase domain of the enzyme activator sensing, nucleotide binding, dimerization, and ribonuclease functions
additional information
structure-function analysis, overview. The KH/KH and kinase extension nuclease (KEN)/KEN interfaces are important in 2',5'-oligoadenylate-dependent enzyme activation
additional information
-
structure-function analysis, overview. The KH/KH and kinase extension nuclease (KEN)/KEN interfaces are important in 2',5'-oligoadenylate-dependent enzyme activation
additional information
-
the enzyme catalytic site, which is responsible for RNA degradation is composed of residues His51, His110, His115, Glu111, Trp54, Asp56, and Tyr62 which are involved in binding the target base. These residues are located on the surface of the molecule, thereby creating a cavity for the substrate
additional information
-
the kinase-like region is required for the ribonuclease activity of the enzyme
Show AA Sequence and Transmembrane Helices (4699 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23700
24000
25000
27660
-
x * 30558, glyosylated enzyme, mass spectrometry, x * 27660, sequence calculation
30558
-
x * 30558, glyosylated enzyme, mass spectrometry, x * 27660, sequence calculation
36000
-
gel filtration, RNase T2, larger forms, MW: 80000, have higher carbohydrate content
45000
62100
-
recombinant truncated enzyme RNase L(1-333) with bound 2'-5'-oligoadenylate, gel filtration
80000
-
gel filtration, RNase T2-L1-5, smaller form, MW: 36000, has smaller carbohydrate content
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
?
-
x * 30558, glyosylated enzyme, mass spectrometry, x * 27660, sequence calculation
dimer
-
the dimer configuration of full-length enzyme arises from the intertwining of two promoters through a 155° twisting action across the ANK domain-PK domain junction, which gives rise to the appearance of an exchange of ANK and PK domains between protomers, back-to-back dimer arrangement. Dimerization of the ANK domain is facilitated by a head-to-tail arrangement with concave surfaces facing inward. Kinase domain-ANK domain contacts, overview
dimer
the enzyme forms a crossed homodimer stabilized by ankyrin (ANK) and kinase homology (KH) domains, which positions two kinase extension nuclease (KEN) domains for asymmetric RNA recognition
dimer
-
the dimer configuration of full-length enzyme arises from the intertwining of two promoters through a 155° twisting action across the ANK domain-PK domain junction, which gives rise to the appearance of an exchange of ANK and PK domains between protomers, back-to-back dimer arrangement. Dimerization of the ANK domain is facilitated by a head-to-tail arrangement with concave surfaces facing inward. Kinase domain-ANK domain contacts, overview
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
comparison of primary, secondary, and tertiary structures, overview
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
dimerization of recombinant, ZMP-domain-containing enzyme can be induced by a small organic molecule, RO-2443. But dimerization of RNase L induced by RO-2443 is not sufficient for activation of ribonuclease activity but requires a conformational rearrangement induced by 2'-5'-oligoadenylate that is distinct from the dimer induced by RO-2443
additional information
-
the estimated secondary structural composition of inactive monomeric RNase L is 44% alpha-helix, 28% beta-sheet, 17% beta-turns and 11% of unordered structures, whereas dimerization causes a slight decrease in alpha-helix and increase in beta-sheet (ca. 2%) content. Enzyme dimerization affects at least three Tyr, five Phe and two Trp residues. The alpha-beta structural switch may fix domain positions in the hinge region (residues ca. 336-363) during homodimer formation, Raman spectroscopy, overview
additional information
3 domains: a RNase active domain, a Ser/Thr-rich domain, and a C-terminal 10 kDa domain
additional information
-
3 domains: a RNase active domain, a Ser/Thr-rich domain, and a C-terminal 10 kDa domain
additional information
3 domains: a RNase active domain, a Ser/Thr-rich domain, and a C-terminal 10 kDa domain
additional information
-
3 domains: a RNase active domain, a Ser/Thr-rich domain, and a C-terminal 10 kDa domain
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
comparison of primary, secondary, and tertiary structures, overview
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
comparison of primary, secondary, and tertiary structures, overview
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
the enzyme shows a conserved alpha/beta core structure, identification of substrate binding regions, overview
additional information
-
comparison of primary, secondary, and tertiary structures, overview
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
consisting of nine alpha helices with a 19-residue disordered sequence (residues 644-662, harboring a 12-residue porcine-specific insertion) between helices alpha3 and alpha4, RNase domain structure, overview. The ANK domain of porcine RNase L adopts a crescent-shaped structure consisting of a stack of nine ankyrin repeats, each possessing a characteristic loop-helix1-loop-helix2-loop architecture
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
enzyme contains the conserved sequences CAS1 and CAS2
additional information
-
comparison of primary, secondary, and tertiary structures, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
additional information
glycoprotein
-
16-17% carbohydrate, 12-13% neutral sugars and 4% glucosamine
glycoprotein
-
12-15% carbohydrate, RNase T2-A: mannose, glucose, RNase T2-B: mannose galactose
glycoprotein
-
RNase T2: 10.2% carbohydrate, RNase T2-L1-5: about 50% carbohydrate
glycoprotein
N-linked glycoprotein, enzyme activity is independent of glycosylation, deglycosylation by EndoH leaving one N-acetyl glucosamine residue at each of the N-glycosylation sites
glycoprotein
RNase Le45 is the N-glycosylated form of RNase Le37, the Ser/Thr-rich domain is highly O-glycosylated
glycoprotein
-
the enzyme is a thermostable glycoprotein with two N-glycosylation sites at Asn74 and at Asn83. Both asparagine residues are part of an Asn-Xaa-Ser/Thr motif which is typical for N-glycosylation site
glycoprotein
-
the enzyme undergoes initial N-linked core glycosylation at four sites, N37, N70, N103 and N123 in the endoplasmic reticulum, four potential N-linked glycosylation sites with the NxS/T consensus sequence in the amino terminal portion of Rny1p: N37KT, N70ET, N103RS and N123DT. The enzyme transport to the Golgi results in the further attachment of high-glycans. Modifications with glycans are dispensable for the nucleolytic enzyme activity. Function of Golgi glycosylation in a T2 RNase as a sorting and secretion signal, overview
glycoprotein
-
contains 2.1% neutral sugars and 2.1 residues/mol glucosamine
additional information
-
RNase LX contains a putative signal for ER retention
additional information
-
the enzymes contain secretory targeting signals, RNase LX contains an ER retention signal sequence
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure of the activity domain of colcin E5, E5-CRD, in complex with immunity protein Im5 at a resolution of 1.15 A is reported
-
wild-type RNase II is crystallized in two crystal forms, diffraction data are collected to 2.44 and 2.75 A resolution, the D209N mutant crystals diffract to 2.74 A
-
purified enzyme, hanging drop vapour diffusion method, mixing of 0.002 ml of 9.2 mg/ml protein in 20 mM acetate, pH 6.0, and 20 mM NaCl, with 0.002 ml of reservoir solution containing 0.2 M NH4NO3 and 15% PEG 3350, equilibration over 0.6 ml of reservoir solution, X-ray diffraction structure determination and analysis at 1.6 A resolution
19 mg/ml wild-type enzyme in complex with 2'-UMP and 3'-UMP, hanging drop vapour diffusion method, reservoir solution contains 0.2 M sodium acetate, 0.1 M sodium cacodylate, pH 6.7, 21% PEG 8000, 10 mM 2'-UMP or 3'-UMP, 4 days, X-ray diffraction structure determination and analysis at 1.48 and 1.77 A resolution, respectively
-
determined in complex with either 5'-AMP, 5'-GMP, or 2'-UMP, 1.8 A resolution, data collections and refinement statistics shown, 5'-GMP and 5'-AMP bind both B1 and B2 sites, 2'-UMP predominantly binds B1 site in the crystallized complex, Trp42, Asn44, and Trp50 involved in base-interaction at the primary B1 site, Gln12, Tyr17, Ser78, Leu79, and Phe89 involved in base-recognition at the B2 subsite
-
purified enzyme, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
-
20 mg/ml purified recombinant wild-type enzyme, hanging drop vapour diffusion method, equal volumes of protein solution, 20 mM citrate, pH 5.0, and reservoir solution, 0.1 M citrate, pH 5.0, 36% w/v PEG 1540, X-ray diffraction structure determination and analysis at 1.65-2.2 A resolution of wild-type enzyme crystals and heavy atom derivatives
enzyme with bound natural activator 2',5'-oligoadenylate and with and without ADP or the nonhydrolysable ATP mimetic AMP-PNP, X-ray diffraction structure determination and analysis at 2.5 A resolution and small-angle X-ray scattering structure determination and analysis at 3.25 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C184R
-
RNASET2C184R, harboring a missense mutation as identified from a patient with cystic leukoencephalopathy, signal is retained within the endoplasmic reticulum
T304A
-
naturally occuring mutation, inactivce mutant AO127. A mutation within codon 118 of the rnaset2 ORF creates a premature stop codon truncating the protein before its second conserved catalytic site, CAS II, resulting in loss of essential catalytic residues and results in a dramatic down-regulation of the rnaset2 messenger RNA
D209N
H672N
K392R
-
the mutation in the kinase ATP binding site of the nezyme results in greatly impaired RNase activity
R163A
action potential aI clamp enzyme mutant, which shows reduced activity compared to the wild-type enzyme
R412A
KH/KH interface enzyme mutant, which shows reduced activity compared to the wild-type enzyme
R427A
activator recognition enzyme mutant, which shows reduced activity compared to the wild-type enzyme
R667A
A105L
significant loss of activity, significant decrease in thermostability
E84A
-
site-directed mutagenesis, decreased kcat, 90% reduced activity compared to the wild-type enzyme
F102A
considerable less stable than the wild-type in guanidine-HCl, significant decrease in thermostability
H83A
-
site-directed mutagenesis, decreased kcat, 80% reduced activity compared to the wild-type enzyme
K87A
-
site-directed mutagenesis, decreased kcat, 45% reduced activity compared to the wild-type enzyme
L73A
-
site-directed mutagenesis, slightly increased catalytic efficiency and 14.5fold decreased binding affinity compared to the wild-type enzyme
N71T
-
site-directed mutagenesis, 2.3fold decreased catalytic efficiency and 7.0fold decreased binding affinity compared to the wild-type enzyme
R74S
-
site-directed mutagenesis, decreased catalytic efficiency and 0.8fold increased binding affinity compared to the wild-type enzyme
V72L
-
site-directed mutagenesis, catalytic efficiency and binding affinity similar to the wild-type enzyme
Y101A
considerable less stable than the wild-type in guanidine-HCl, significant decrease in thermostability
D51A
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
D51E
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
D51K
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
D51N
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
D51Q
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
D51S
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
D51T
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
F101A
-
site-directed mutagenesis, below 1% activity compared to the wild-type enzyme
F101I
-
site-directed mutagenesis, 3.8% activity compared to the wild-type enzyme
F101K
-
site-directed mutagenesis, below 1% activity compared to the wild-type enzyme
F101L
-
site-directed mutagenesis, 20% activity compared to the wild-type enzyme
F101Q
-
site-directed mutagenesis, below 1% activity compared to the wild-type enzyme
F101W
-
site-directed mutagenesis, 7% activity compared to the wild-type enzyme
Q32D
-
site-directed mutagenesis, 26% activity compared to the wild-type enzyme
Q32E
-
site-directed mutagenesis, 78% activity compared to the wild-type enzyme
Q32F
-
site-directed mutagenesis, 9.3% activity compared to the wild-type enzyme
Q32L
-
site-directed mutagenesis, 112% activity compared to the wild-type enzyme
Q32N
-
site-directed mutagenesis, 21% activity compared to the wild-type enzyme
Q32T
-
site-directed mutagenesis, 125% activity compared to the wild-type enzyme
Q32V
-
site-directed mutagenesis, 39% activity compared to the wild-type enzyme
W49F
Y57W
N37Q/N70Q/N103Q/N123Q
-
site-directed mutagenesis of N-glycosylation sites, the mutant is mislocated to the vacuole
W399R
-
site-directed mutagenesis, the mutant is mislocated to the vacuole
P509L
-
mutant contains a reduced RNase activity, the spindle-kinetochore interaction is abnormal in mutant cells, associated with mitotic arrest at a pre-anaphase stage
H109F
site-directed mutagenesis, 35% activity compared to the wild-type enzyme
H134F
site-directed mutagenesis, 49% activity compared to the wild-type enzyme
H39F
site-directed mutagenesis, conserved active site residue, 0.18% activity compared to the wild-type enzyme
H92F
site-directed mutagenesis, conserved active site residue, 0.21% activity compared to the wild-type enzyme
H97F
site-directed mutagenesis, conserved active site residue, 0.12% activity compared to the wild-type enzyme
K390R
-
the mutation in the kinase ATP binding site of the nezyme results in greatly impaired RNase activity
additional information
H672N
RNA cleavage enzyme mutant, which shows reduced activity compared to the wild-type enzyme. The H672N mutation eliminates the proton transfer but preserves the H-bonding and space-filling character of histidine. Thus, the H672N mutant interacts with RNA analogous to the wild-type protein but without cleaving the RNA. A single H672N mutant is a potent in trans activator for wild-type RNase L, whereas a double H672N mutant is inactive
additional information
-
transposon mutagenesis analysis of abiotic surface-colonization of wild-type and enzyme-deletion mutant strain 98-37-09, the mutant exhibits reduced expression of 29 genes, 15 of which are predicted to be associated with bacterial attachment and surface-associated motility, overview
additional information
-
transposon mutagenesis analysis of abiotic surface-colonization of wild-type and enzyme-deletion mutant strain 98-37-09, the mutant exhibits reduced expression of 29 genes, 15 of which are predicted to be associated with bacterial attachment and surface-associated motility, overview
-
additional information
-
alteration of the RNase I by mutantion of 3 amino acids to RNase M sequence and confer of enzyme properties, comparison of RNase M mutant strain activities
additional information
-
expression of the enzyme in transgenic Nicotiana alata plants allows the plants to accept pollen from another Nicotiana alata self-incompatible plant
additional information
-
in addition the selenomethionine-derivatized D209N protein is produced
additional information
-
alteration of the RNase I by mutantion of 3 amino acids to RNase M sequence and confer of enzyme properties, comparison of RNase M mutant strain activities
-
additional information
-
deletion mutant NDELTA385 is a constitutively active form of RNase L
additional information
-
generation of the truncated enzyme mutant RNase L(1-333) by insering a TEV cleavage site into the recombinant enzyme and cleaving it into two proteins, truncated enzyme comprising residues 432-741 shows proteolytic stability and no change in oligomeric state in the absence and presence ofMg2+ and ATP
additional information
-
transgenic plants expressing the Escherichia coli gene instead of the endogenous gene do not reject the pollen of another self-incompatibele Nicotiana alata plant
additional information
-
construction of enzyme mutants which possess designed substrate specificity, conversion of the base-nonspecific wild-type to base-specific mutants
additional information
-
the DELAT18N mutant lacking the 18 N-terminal amino acids of the signal peptide is catalytically inactive
additional information
transgenic Nicotiana benthamiana plants carrying the uidA reporter gene under the control of a 900-bp RNaseLER promoter sequence express the reporter gene predominantly in guard cells and trichomes
additional information
-
transgenic Nicotiana benthamiana plants carrying the uidA reporter gene under the control of a 900-bp RNaseLER promoter sequence express the reporter gene predominantly in guard cells and trichomes
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
50
64
-
30 min, pH 4.2: 95% inactivation, pH 6.6: 49% inactivation, pH 10.0: 64% inactivation
70
100
-
5 min, different pH values and ionic strengths, complete inactivation
50
-
pH 4.5, 1 h, soluble enzyme: about 29% loss of activity, immobilized enzyme: about 10% loss of activity
50
-
fully active up to 50°C, then decrease in activity with increase in temperature, no acitivity at 65°
70
-
pH 4.5, 1 h, soluble form: complete loss of activity, immobilized form: about 40% loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the wild-type enzyme remains intact during incubation with chymotrypsin for 8 h (pH 8.0, 37°C). Trypsin causes a time-dependent decrease of the RNase MC1 band concomitant with the increase of one peptide. Mutant Y101A is completely degraded by chymotrypsin and trypsin after 2 h. Mutant F102A is also susceptible to protease degradation. In mutants A105L, D107A, P125A, G127A, G144A, V165A, F190A and G173A the degradation pattern is similar to the wild-type.
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
mutants Y101A (guanidine-HCl concentration at the midpoint of the transition is 1.59 M) and F102A (guanidine-HCl concentration at the midpoint of the transition is 1.64 M) are considerable less stable than the wild-type (guanidine-HCl concentration at the midpoint of the transition is 2.57 M). In mutant P125A guanidine-HCl concentration at the midpoint of the transition is 2.11 M, in mutant G127A guanidine-HCl concentration at the midpoint of the transition is 2.12 M, in mutant G173A guanidine-HCl concentration at the midpoint of the transition is 2.56 M
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
photooxidation, pH-dependence of photooxidation-inactivation in presence of methylene Blue, 2',3'-AMP prevents inactivation
-
134492
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
extracts of different parts of the plant are precipitated with ammonium sulfate, the resuspended and dialysed protein fractions are purified using CM-cellulose, DEAE-Sephadex A-25 and Sephadex G-50 columns
-
preparation of microsomes, protoplasts, vacuoles, cell culture supernatant, purification of RNase LE, LX, and LV-1-3, different methods, 1800-4400fold, overview
-
recombinant GST-fusion dominant negative mouse enzyme from Escherichia coli strain BL21 by glutathione affinity chromatography
-
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli by glutathione affinity chromatography and TEV-cleavage
-
recombinant His-tagged enzyme by metal affinity chromatography, deglycosylation, concanavalin A affinity chromatography and gel filtration
recombinant His6-tagged enzyme variants from Escherichia coli strain BL21(DE3) or Spodoptera frugiperda Sf9 insect cells by ultracentrifugation, nickel affinity chromatography and gel filtration, dialysis, anion exchange chromatography, clevage by TEV protease and again nickel affinity chromatography, gel filtration and
-
recombinant mutant enzymes from culture supernatant of transformed Saccharomyces cerevisiae
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography and dialysis
-
using a CM-cellulose column, a DEAE-cellulose column and a Sephadex-G100 column
-
using a HisTrap-Chelating HP column, the His-tag is removed in some batches, using biotinylated thrombin
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, constitutively expressed single copy gene, quantitative real-time RT-PCR expression analysis, expression of YFP-tagged enzyme under control of the 35S promoter in vector pCP60 in Nicotiana benthamiana leaves via transfection with Agrobacterium tumefaciens
DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
enzymes are S-gene products, cloning of RNases Le and LX, DNA and amino acid sequence determination and analysis
-
expressed in Escherichia coli, cloning vector pCR2-1, transformation of binary plasmid constructs into Agrobacterium tumefaciens strain LBA 4404, T2 progeny analyzed after plant transformation
expressed in Escherichia coli, expression plasmid pPIC9K, host strain GS115
-
expression of FLAG-tagged wild-type, R667A mutant, and NDELTA385 deletion enzyme mutant in HeLa-M cells
-
expression of GFP-tagged wild-type enzyme and unglycosylated enzyme mutant N37Q/N70Q/N103Q/N123Q in the dolichol pathway-defective alg5DELTA and Golgi-glycosylation-deficient och1DELTA cells and ocalization to the vacuole
-
expression of mutant enzymes in Saccharomyces cerevisiae R27-7C-1C, secretion to culture medium
-
expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expression of recombinant GST-fusion dominant negative mouse enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain DH5alpha
-
expression of wild-type and mutant enzymes in HeLa-M cell and in Escherichia coli as TEV-cleavable GST fusion proteins
-
expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain R27-7C-1C
-
mutants A105L, D107A, P125A, G127A, G144A, V165A and F190A are expressed in Escherichia coli. Mutants Y101A, F102A, L162A and G173A are expressed in Pichia pastoris
overexpression of wild-type and mutant enzymes in Escherichia coli BL21(DE3)
-
recombinant expression of His6-tagged enzyme with or without TEV cleavage site inserted after residue 333 and the amino acid sequence of ZMP comprised residues 15 to 129 of zebrafish MDMX with two mutations L46V and V95L, in Escherichia coli strain BL21(DE3) or in Spodoptera frugiperda Sf9 insect cells. The zebrafish sequence ZMP is a unique dimerization inducing domain and represents a tool protein for solving crystal structures of inhibitors binding to the p53-interacting domain of MDMX
-
rna gene encoding the enzyme contains a UGA nonsense codon at position 5 and is a multiply altered form of RNase I gene
-
RNase P is a ribonucleoprotein consisting of a large RNA and protein components, RNA P4 helix samples are prepared by in vitro transcription reactions
-
sequencing of a positional candidate zgc:113369, equivalent to rnaset2, expresison of myc-tagged wild-type and mutants in HEK-293 cells, phenotypes, overview
-
untagged recombinant human RNase L in a baculovirus vector is expressed in SF21 insect cells, into pcDNA3 vectors for stable transfection of HeLa cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
overexpression of RNASET2 in consequence of the activation of HIF-1alpha.
reduction in the level of RNase T2 by Tax protein from human T cell leukemia virus type 1
-
RNase Dre2 expressed in all developmental stages and peaking at 72 h, signal is lower at 5 and 12 h
RNase X25 enzyme expression is elevated in response to nutritional and oxidative stresses
significantly higher expression of RNASET2, HIF-1alpha, and its target CA IX in poorly differentiated than in well-differentiated LuNENs
strong expression of RNase Dre1 during all developmental stages analyzed (2, 5, 12, 24, 72 h after fertilization), with a peak of expression at 72 hours
treatments with abscisic acid, ethylene or other abiotic and biotic stress factors do not affect RNaseLER expression significantly
RNase X25 enzyme expression is elevated in response to nutritional and oxidative stresses
-
RNase X25 enzyme expression is elevated in response to nutritional and oxidative stresses
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
isolate could be a novel renewable source of DNase-free RNase enzyme
medicine
-
it will be important, for proving advantageous in vaccines, to determine whether mutations in the RNA structure associated with the inhibition of RNAse L attenuate polyviruses or other group C enteroviruses in vivo
additional information
additional information
-
the enzyme may be an effective target for the intervention of biomaterial colonization, and consequently limit the organisms transmission within the hospital setting
additional information
-
the enzyme may be an effective target for the intervention of biomaterial colonization, and consequently limit the organisms transmission within the hospital setting
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Uchida, T.; Egami, F.
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Aspergillus oryzae
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Aspergillus phoenicis
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Aspergillus phoenicis, Escherichia coli
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Imada, A.; Hunt, J.W.; van de Sande, H.; Sinskey, A.J.; Tannenbaum, S.R.
Purification and properties of an intracellular ribonuclease from Candida lipolytica
Biochim. Biophys. Acta
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Yarrowia lipolytica
brenda
Pietrzak, M.; Cudny, H.; Maluszynski, M.
Purification and properties of two ribonucleases and a nuclease from barley seeds
Biochim. Biophys. Acta
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Hordeum vulgare
brenda
Shimada, H.; Inokuchi, N.; Oduwaki, H.; Koyama, T.; Irie, M.
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Agric. Biol. Chem.
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Lentinula edodes
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Kawata, Y.; Hamaguchi, K.
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Aspergillus oryzae
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Watanabe, H.; Fauzi, H.; Iwama, M.; Onda, T.; Ohgi, K.; Irie, M.
Base non-specific acid ribonuclease from Irpex lacteus, primary structure and phylogenetic relationships in RNase T2 family enzymes
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Irpex lacteus
brenda
Ohgi, K.; Takeuchi, M.; Iwama, M.; Irie, M.
Enzymatic properties of double mutant enzymes at Asp51 and Trp49 and Asp51 and Tyr57 of RNase Rh from Rhizopus niveus
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61
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Rhizopus niveus
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Leon, D.; Gite, S.; Shankar, V.
Partial purification and immobilization of ribonuclease T2
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Aspergillus oryzae
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Inokuchi, N.; Kobayashi, H.; Miyamoto, M.; Koyama, T.; Iwama, M.; Ohgi, K.; Irie, M.
Primary structure of base non-specific and acid ribonuclease from bullfrog (Rana catesbeiana)
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Lithobates catesbeianus
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Ohgi, K.; Takeuchi, M.; Iwama, M.; Irie, M.
Enzymatic properties of mutant enzymes at Trp49 and Tyr57 of RNase Rh from Rhizopus niveus
J. Biochem.
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Rhizopus niveus
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Watanabe, H.; Narumi, H.; Inaba, T.; Ohgi, K.; Irie, M.
Purification, some properties, and primary structure of a base non-specific ribonuclease from Oyster (Crussdstrea grigus)
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Crassostrea gigas
brenda
Inokuchi, N.; Saitoh, S.; Kobayashi, H.; Itagaki, T.; Koyama, T.; Uchiyama, S.; Iwama, M.; Ohgi, K.; Irie, M.
Characterization and primary structure of a base non-specific and acid ribonuclease from Dictostelium discoideum
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Dictyostelium discoideum
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Ohgi, K.; Takeuchi, M.; Iwama, M.; Irie, M.
Enzymatic properties of mutant forms of RNase Rh from Rhizopus niveus as to Asp51
J. Biochem.
119
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Rhizopus niveus
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Rhizopus niveus
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Yagi, H.; Kobayashi, H.; Inokuchi, N.; Koyama, T.; Irie, M.
Purification, and properties of a base non-specific acid ribonuclease from bullfrog (Rana cateseiana)
Biol. Pharm. Bull.
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Lithobates catesbeianus
brenda
Suzuki, A.; Yao, M.; Tanaka, I.; Numata, T.; Kikukawa, S.; Yamasaki, N.; Kimura, M.
Crystal structures of the ribonuclease MC1 from bitter gourd seeds, complexed with 2'-UMP or 3'-UMP, reveal structural basis for uridine specificity
Biochem. Biophys. Res. Commun.
275
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Momordica charantia
brenda
Ohgi, K.; Kudo, S.; Takeuchi, M.; Iwama, M.; Irie, M.
Enzymatic properties of phenylalanine 101 mutant enzyme of ribonuclease Rh from Rhizopus niveus
Biosci. Biotechnol. Biochem.
64
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2000
Rhizopus niveus
brenda
Numata, T.; Kashiba, T.; Hino, M.; Funatsu, G.; Ishiguro, M.; Yamasaki, N.; Kimura, M.
Expression and mutational analysis of amino acid residues involved in catalytic activity in a ribonuclease MC1 from the seeds of bitter gourd
Biosci. Biotechnol. Biochem.
64
603-605
2000
Momordica charantia
brenda
Kobayashi, H.; Itagaki, T.; Inokuchi, N.; Ohgi, K.; Wada, T.; Iwama, M.; Irie, M.
A new type of RNase T2 ribonuclease in two Basidiomycetes fungi, Lentinus edodes and Irpex lacteus
Biosci. Biotechnol. Biochem.
67
2307-2310
2003
Lentinula edodes (Q7Z869), Lentinula edodes, Irpex lacteus (Q8LW55), Irpex lacteus
brenda
Ohgi, K.; Iwama, M.; Inokuchi, N.; Irie, M.
Enzymatic properties of glutamine 32 mutants of RNase Rh from Rhizopus niveus, a trial to alter the most preferential inter-nucleotidic linkages of RNase Rh
Biosci. Biotechnol. Biochem.
67
570-576
2003
Rhizopus niveus
brenda
Naskalski, J.; Anyszek, T.; Surdacka, E.; Hoyer, B.; Sulowicz, W.
Acid ribonuclease and alkaline ribonuclease isoenzymes in plasma of patients with decreased glomerular filtration rate
Clin. Chem. Lab. Med.
42
279-282
2004
Homo sapiens
brenda
Tanaka, N.; Arai, J.; Inokuchi, N.; Koyama, T.; Ohgi, K.; Irie, M.; Nakamura, K.T.
Crystal structure of a plant ribonuclease, RNase LE
J. Mol. Biol.
298
859-873
2000
Solanum lycopersicum (P80022), Solanum lycopersicum
brenda
Abel, S.; Kock, M.
Secretory acid ribonucleases from tomato, Lycopersicon esculentum Mill
Methods Enzymol.
341
351-368
2001
Arabidopsis thaliana, Solanum lycopersicum, Momordica charantia, Zinnia elegans, Nicotiana glutinosa (Q9SSV1)
brenda
Irie, M.; Ohgi, K.
Ribonuclease T2
Methods Enzymol.
341
42-55
2001
Aeromonas hydrophila, Aspergillus oryzae, Aspergillus phoenicis, Bos taurus, Gallus gallus, Classical swine fever virus, Crassostrea gigas, Cucumis sativus, Cucumis melo, Dictyostelium discoideum, Drosophila melanogaster, Escherichia coli, Irpex lacteus, Lentinula edodes, Luffa aegyptiaca, Solanum lycopersicum, Momordica charantia, Physarum polycephalum, Lithobates catesbeianus, Rattus norvegicus, Rhizopus niveus, Sus scrofa, Tetrahymena pyriformis, Trichoderma viride, Nicotiana alata, squid, Phytophthora nicotianae
brenda
Subbarayan, P.R.; Deutscher, M.P.
Escherichia coli RNase M is a multiply altered form of RNase I
RNA
7
1702-1707
2001
Escherichia coli, Escherichia coli CA265
brenda
Kimura, K.; Numata, T.; Kakuta, Y.; Kimura, M.
Amino acids conserved at the C-terminal half of the ribonuclease T2 family contribute to protein stability of the enzymes
Biosci. Biotechnol. Biochem.
68
1748-1757
2004
Momordica charantia (P23540), Momordica charantia
brenda
Suzuki, R.; Kanno, S.; Ogawa, Y.; Iwama, M.; Tsuji, T.; Ohgi, K.; Irie, M.
On a salmon (Oncorhynchus [corrected] keta) liver RNase, belonging to RNase T2 family: primary structure and some properties
Biosci. Biotechnol. Biochem.
69
343-352
2005
Oncorhynchus keta
brenda
Amblar, M.; Arraiano, C.M.
A single mutation in Escherichia coli ribonuclease II inactivates the enzyme without affecting RNA binding
FEBS J.
272
363-374
2005
Escherichia coli
brenda
Sana, B.; Ghosh, D.; Saha, M.; Mukherjee, J.
Purification and characterization of an extracellular, uracil specific ribonuclease from a Bizionia species isolated from the marine environment of the Sundarbans
Microbiol. Res.
163
31-38
2008
Bacteroides sp.
brenda
Cheng, Z.F.; Deutscher, M.P.
An important role for RNase R in mRNA decay
Mol. Cell
17
313-318
2005
Escherichia coli
brenda
Kock, M.; Gross, N.; Stenzel, I.; Hause, G.
Phloem-specific expression of the wound-inducible ribonuclease LE from tomato (Lycopersicon esculentum cv. Lukullus)
Planta
219
233-242
2004
Solanum lycopersicum (P80022), Solanum lycopersicum
brenda
Kawano, S.; Kakuta, Y.; Nakashima, T.; Kimura, M.
Crystal structures of the Nicotiana glutinosa ribonuclease NT in complex with nucleoside monophosphates
J. Biochem.
140
375-381
2006
Nicotiana glutinosa
brenda
Koeck, M.; Stenzel, I.; Zimmer, A.
Tissue-specific expression of tomato Ribonuclease LX during phosphate starvation-induced root growth
J. Exp. Bot.
57
3717-3726
2006
Solanum lycopersicum (P80196), Solanum lycopersicum
brenda
Getz, M.M.; Andrews, A.J.; Fierke, C.A.; Al-Hashimi, H.M.
Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation
RNA
13
251-266
2007
Bacillus subtilis
brenda
McVey, C.E.; Amblar, M.; Barbas, A.; Cairrao, F.; Coelho, R.; Romao, C.; Arraiano, C.M.; Carrondo, M.A.; Frazao, C.
Expression, purification, crystallization and preliminary diffraction data characterization of Escherichia coli ribonuclease II (RNase II)
Acta Crystallogr. Sect. F
F62
684-687
2006
Escherichia coli
brenda
Luna-Chavez, C.; Lin, Y.L.; Huang, R.H.
Molecular basis of inhibition of the ribonuclease activity in colicin E5 by its cognate immunity protein
J. Mol. Biol.
358
571-579
2006
Escherichia coli
brenda
Han, J.Q.; Townsend, H.L.; Jha, B.K.; Paranjape, J.M.; Silverman, R.H.; Barton, D.J.
A phylogenetically conserved RNA structure in the poliovirus open reading frame inhibits the antiviral endoribonuclease RNase L
J. Virol.
81
5561-5572
2007
Homo sapiens
brenda
Naito, T.; Yokogawa, T.; Kim, H.S.; Matsuda, A.; Sasaki, T.; Fukushima, M.; Kitade, Y.; Wataya, Y.
A novel apoptotic pathway of 3-Ethynylcytidine(ECyd) involving the inhibition of RNA synthesis--the possibility of RNase L activated pathway as a target of ECyd
Nucleic Acids Symp. Ser.
51
435-436
2007
Mus musculus
brenda
Gomes-Filho, E.; Lima, C.R.; Costa, J.H.; da Silva, A.C.; da Guia Silva Lima, M.; de Lacerda, C.F.; Prisco, J.T.
Cowpea ribonuclease: properties and effect of NaCl-salinity on its activation during seed germination and seedling establishment
Plant Cell Rep.
27
147-157
2008
Vigna unguiculata
brenda
Murakami, H.; Goto, D.B.; Toda, T.; Chen, E.S.; Grewal, S.I.; Martienssen, R.A.; Yanagida, M.
Ribonuclease activity of Dis3 is required for mitotic progression and provides a possible link between heterochromatin and kinetochore function
PLoS ONE
3
e317
2007
Schizosaccharomyces pombe
brenda
Barbas, A.; Matos, R.G.; Amblar, M.; Lpez-Vinas, E.; Gomez-Puertas, P.; Arraiano, C.M.
New insights into the mechanism of RNA degradation by ribonuclease II identification of the residue responsible for setting the RNase II end product
J. Biol. Chem.
283
13070-13076
2008
Escherichia coli
brenda
Hillwig, M.; Rizhsky, L.; Wang, Y.; Umanskaya, A.; Essner, J.; MacIntosh, G.
Zebrafish RNase T2 genes and the evolution of secretory ribonucleases in animals
BMC Evol. Biol.
9
170
2009
Danio rerio (B8XY54), Danio rerio (B8XY55), Danio rerio (B8XY56), Danio rerio
brenda
Koethke, S.; Koeck, M.
The Solanum lycopersicum RNaseLER is a class II enzyme of the RNase T2 family and shows preferential expression in guard cells
J. Plant Physiol.
168
840-847
2011
Solanum lycopersicum (A0AQW5), Solanum lycopersicum
brenda
Hillwig, M.S.; Contento, A.L.; Meyer, A.; Ebany, D.; Bassham, D.C.; Macintosh, G.C.
RNS2, a conserved member of the RNase T2 family, is necessary for ribosomal RNA decay in plants
Proc. Natl. Acad. Sci. USA
108
1093-1098
2011
Arabidopsis thaliana
brenda
Haud, N.; Kara, F.; Diekmann, S.; Henneke, M.; Willer, J.R.; Hillwig, M.S.; Gregg, R.G.; Macintosh, G.C.; Gaertner, J.; Alia, A.; Hurlstone, A.F.
rnaset2 mutant zebrafish model familial cystic leukoencephalopathy and reveal a role for RNase T2 in degrading ribosomal RNA
Proc. Natl. Acad. Sci. USA
108
1099-1103
2011
Danio rerio
brenda
Luhtala, N.; Parker, R.
T2 Family ribonucleases: ancient enzymes with diverse roles
Trends Biochem. Sci.
35
253-259
2010
Aspergillus niger, Aspergillus oryzae, Bovine viral diarrhea virus 1, Classical swine fever virus, Entamoeba histolytica, Homo sapiens, Rhizopus niveus, Schistosoma mansoni
brenda
Polakowski, N.; Han, H.; Lemasson, I.
Direct inhibition of RNAse T2 expression by the HTLV-1 viral protein Tax
Viruses
3
1485-1500
2011
Homo sapiens
brenda
Kriz, M.; Snasel, J.; Kopecky, V.; Pav, O.; Rosenberg, I.; Stepanek, J.
Structural changes of human RNase L upon homodimerization investigated by Raman spectroscopy
Biochim. Biophys. Acta
1824
1039-1044
2012
Homo sapiens
brenda
Garvie, C.W.; Vasanthavada, K.; Xiang, Q.
Mechanistic insights into RNase L through use of an MDMX-derived multi-functional protein domain
Biochim. Biophys. Acta
1834
1562-1571
2013
Homo sapiens
brenda
Gupta, A.; Rath, P.C.
Expression of mRNA and protein-protein interaction of the antiviral endoribonuclease RNase L in mouse spleen
Int. J. Biol. Macromol.
69
307-318
2014
Mus musculus, Mus musculus Swiss albino
brenda
de Leeuw, M.; Gonzalez, A.; Lanir, A.; Roiz, L.; Smirnoff, P.; Schwartz, B.; Shoseyov, O.; Almog, O.
The 1.8 A crystal structure of ACTIBIND suggests a mode of action for T2 ribonucleases as antitumorigenic agents
J. Med. Chem.
55
1013-1020
2012
Homo sapiens, Rattus norvegicus
brenda
Chakrabarti, A.; Ghosh, P.K.; Banerjee, S.; Gaughan, C.; Silverman, R.H.
RNase L triggers autophagy in response to viral infections
J. Virol.
86
11311-11321
2012
Homo sapiens
brenda
Banerjee, S.; Chakrabarti, A.; Jha, B.K.; Weiss, S.R.; Silverman, R.H.
Cell-type-specific effects of RNase L on viral induction of beta interferon
mBio
5
e00856
2014
Mus musculus
brenda
Huang, H.; Zeqiraj, E.; Dong, B.; Jha, B.K.; Duffy, N.M.; Orlicky, S.; Thevakumaran, N.; Talukdar, M.; Pillon, M.C.; Ceccarelli, D.F.; Wan, L.C.; Juang, Y.C.; Mao, D.Y.; Gaughan, C.; Brinton, M.A.; Perelygin, A.A.; Kourinov, I.; Guarne, A.; Silverman, R.H.; Sicheri, F.
Dimeric structure of pseudokinase RNase L bound to 2-5A reveals a basis for interferon-induced antiviral activity
Mol. Cell
53
221-234
2014
Homo sapiens, Sus scrofa
brenda
Thorn, A.; Steinfeld, R.; Ziegenbein, M.; Grapp, M.; Hsiao, H.H.; Urlaub, H.; Sheldrick, G.M.; Gaertner, J.; Kraetzner, R.
Structure and activity of the only human RNase T2
Nucleic Acids Res.
40
8733-8742
2012
Homo sapiens (O00584), Homo sapiens
brenda
Zhang, A.; Dong, B.; Doucet, A.J.; Moldovan, J.B.; Moran, J.V.; Silverman, R.H.
RNase L restricts the mobility of engineered retrotransposons in cultured human cells
Nucleic Acids Res.
42
3803-3820
2014
Homo sapiens
brenda
Ambrosio, L.; Morriss, S.; Riaz, A.; Bailey, R.; Ding, J.; MacIntosh, G.C.
Phylogenetic analyses and characterization of RNase X25 from Drosophila melanogaster suggest a conserved housekeeping role and additional functions for RNase T2 enzymes in protostomes
PLoS ONE
9
e105444
2014
Drosophila melanogaster, Drosophila melanogaster w1118/w1118, Protostomia
brenda
Jacobs, A.C.; Blanchard, C.E.; Catherman, S.C.; Dunman, P.M.; Murata, Y.
An ribonuclease T2 family protein modulates Acinetobacter baumannii abiotic surface colonization
PLoS ONE
9
e85729
2014
Acinetobacter baumannii, Acinetobacter baumannii 98-37-09
brenda
Han, Y.; Donovan, J.; Rath, S.; Whitney, G.; Chitrakar, A.; Korennykh, A.
Structure of human RNase L reveals the basis for regulated RNA decay in the IFN response
Science
343
1244-1248
2014
Homo sapiens (Q05823), Homo sapiens
brenda
Shcherbik, N.
Golgi-mediated glycosylation determines residency of the T2 RNase Rny1p in Saccharomyces cerevisiae
Traffic
14
1209-1227
2013
Saccharomyces cerevisiae
brenda
Uccella, S.; La Rosa, S.; Scaldaferri, D.; Monti, L.; Maragliano, R.; Sorrenti, E.; Gariboldi, M.; Taramelli, R.; Sessa, F.; Acquati, F.
New insights into hypoxia-related mechanisms involved in different microvascular patterns of bronchopulmonary carcinoids and poorly differentiated neuroendocrine carcinomas. Role of ribonuclease T2 (RNASET2) and HIF-1alpha
Hum. Pathol.
79
66-76
2018
Homo sapiens (O00584)
brenda
Ferguson, B.J.; Newland, S.A.; Gibbs, S.E.; Tourlomousis, P.; Fernandes dos Santos, P.; Patel, M.N.; Hall, S.W.; Walczak, H.; Schramm, G.; Haas, H.; Dunne, D.W.; Cooke, A.; Zaccone, P.
The Schistosoma mansoni T2 ribonuclease omega-1 modulates inflammasome-dependent IL-1beta secretion in macrophages
Int. J. Parasitol.
45
809-813
2015
Schistosoma mansoni (Q2Y2H5), Schistosoma mansoni
brenda
Huang, J.; Liu, P.; Wang, G.
Regulation of mitochondrion-associated cytosolic ribosomes by mammalian mitochondrial ribonuclease T2 (RNASET2)
J. Biol. Chem.
293
19633-19644
2018
Homo sapiens (C0HKG5), Mus musculus (C0HKG5), Mus musculus
brenda
Ke, X.D.; Shen, S.; Song, L.J.; Yu, C.X.; Kikuchi, M.; Hirayama, K.; Gao, H.; Wang, J.; Yin, X.; Yao, Y.; Liu, Q.; Zhou, W.
Characterization of Schistosoma japonicum CP1412 protein as a novel member of the ribonuclease T2 molecule family with immune regulatory function
Parasit. Vectors
10
89
2017
Schistosoma japonicum (Q6PYW1), Schistosoma japonicum
brenda
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