Any feedback?
Information on EC 2.3.2.8 - arginyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9ZT48
for references in articles please use BRENDA:EC2.3.2.8Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.2.8 arginyltransferaseIUBMB Comments
Requires 2-sulfanylethan-1-ol (2-mercaptoethanol) and a univalent cation. Peptides and proteins containing an N-terminal glutamate, aspartate or cystine residue can act as acceptors.
Specify your search results
Word Map
- 2.3.2.8
-
arginylation
-
2.5.1.18
-
rx:glutathione
- rx
-
n-degrons
-
polyubiquitylates
- medicine
- agriculture
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
arginyltransferase, r-transferase, arginyl-trna protein transferase, arginyl-trna-protein transferase, arginyl transferase, arg-transferase, arginyltransferase 1, arginyl-transferase, arginyl-trna:protein arginyltransferase, ate1-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
arginyl tRNA transferase
-
-
-
-
arginyl-transfer ribonucleate-protein aminoacyltransferase
-
-
-
-
arginyl-transfer ribonucleate-protein transferase
-
-
-
-
arginyl-tRNA protein transferase
-
-
-
-
L-arginyltransferase
-
-
-
-
R-transferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arginyl-tRNAArg:protein arginyltransferase
Requires 2-sulfanylethan-1-ol (2-mercaptoethanol) and a univalent cation. Peptides and proteins containing an N-terminal glutamate, aspartate or cystine residue can act as acceptors.
CAS REGISTRY NUMBER
COMMENTARY
37257-24-2
-
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
L-arginyl-tRNAArg + EBP
tRNAArg + L-arginyl-[EBP]
Pseudomonas syringae ethylene response factor 72 (EBP) is a putative substrate for ATE1
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
-
-
?
L-arginyl-tRNAArg + RIN4
tRNAArg + L-arginyl-[RIN4]
Pseudomonas syringae 1-interacting protein 4 (RIN4) is a putative substrate for ATE1
-
-
?
L-arginyl-tRNAArg + VRN2
tRNAArg + L-arginyl-[VRN2]
Pseudomonas syringae vernalization 2 protein (VRN2) is a putative substrate for ATE1
-
-
?
additional information
?
-
putative substrates of ATE are identified among Nt Met-Cys proteins. N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates
-
-
-
L-arginyl-tRNAArg + ERF-VII peptide
tRNAArg + L-arginyl-[ERF-VII peptide]
after N-terminal Cys-sulfinic acid formation on ERF-VII peptide through plant cysteine oxidase. An ERF-VII peptide with an N-terminal Gly does not accept Arg, whereas an N-terminal Asp accepts Arg, independent of the presence of PCO1 or 4. A peptide comprising an N-terminal Cys-sulfonic acid is also shown to be a substrate for ATE1, again independent of the presence of PCO1 or 4. Proposed arginylation requirements for the Arg/Cys branch of the N-end rule pathway
-
-
?
L-arginyl-tRNAArg + ERF-VII peptide
tRNAArg + L-arginyl-[ERF-VII peptide]
after N-terminal Cys-sulfinic acid formation on ERF-VII peeptide through plant cysteine oxidase. C-terminally biotinylated RAP22-13 peptides (H2N-XGGAIISDFIPP(PEG)K(biotin)-NH2) where the N-terminal residue, X, constitutes Gly, Asp, Cys or Cys-sulfonic acid are subjected to the arginylation assay in the presence or absence of PCO1/4. An ERF-VII peptide with an N-terminal Gly does not accept Arg, whereas an N-terminal Asp accepts Arg, independent of the presence of PCO1 or 4. A peptide comprising an N-terminal Cys-sulfonic acid is also shown to be a substrate for ATE1, again independent of the presence of PCO1 or 4. Arginylation of the 12-mer peptide substrates, peptide sequences, overview
-
-
?
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
L-arginyl-tRNAArg + ERF-VII peptide
tRNAArg + L-arginyl-[ERF-VII peptide]
after N-terminal Cys-sulfinic acid formation on ERF-VII peptide through plant cysteine oxidase. An ERF-VII peptide with an N-terminal Gly does not accept Arg, whereas an N-terminal Asp accepts Arg, independent of the presence of PCO1 or 4. A peptide comprising an N-terminal Cys-sulfonic acid is also shown to be a substrate for ATE1, again independent of the presence of PCO1 or 4. Proposed arginylation requirements for the Arg/Cys branch of the N-end rule pathway
-
-
?
L-arginyl-tRNAArg + protein
tRNAArg + L-arginyl-[protein]
-
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
plant cysteine oxidases
i.e. PCO dioxygenase, dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication
malfunction
metabolism
physiological function
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
malfunction
RAP2.12 stabilization in ate1 ate2 double-null mutant plant lines implicates ATE1 as an ERF-VII-targeting arginyl transferase in vivo
malfunction
the relative abundance of methylesterase 10 (MES10), nucleoside diphosphate kinase family protein (NDPK1), and two asparagine synthetases (ASNs) is augmented in ate1/ate2 mutants. Disrupted ATE1 in dls1 mutants shows an extremely slow age-dependent, dark-induced leaf senescence, phenotype. Double mutant for AtATE1 and AtATE2 (ate1.ate2) displays lost sensitivity to hormone abscisic acid and consequently uncontrolled seed germination and establishment. Arabidopsis ate1/ate2 or prt6 mutants cannot degrade ERFVII, and as a consequence show increased expression of hypoxia-responsive genes involved in fermentation and sugar consumption even under oxygen-rich conditions
metabolism
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. The N-recognin E3 ligase PRT6 and AtATE1 and AtATE2 are involved in seed germination controlled by abscisic acid. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII)
metabolism
submergence-induced hypoxia in plants (e.g. flooded plants) results in stabilization of group VII ethylene response factors (ERF-VIIs), which aid survival under these adverse conditions. ERF-VII stability is controlled by the N-end rule pathway, which proposes that ERF-VII N-terminal cysteine oxidation in normoxia enables arginylation followed by proteasomal degradation. The plant cysteine oxidases (PCOs) are identified as catalysts of this oxidation. ERF-VII stabilization in hypoxia presumably arises from reduced PCO activity. PCO dioxygenase activity produces Cys-sulfinic acid at the N-terminus of an ERF-VII peptide, which then undergoes efficient arginylation by an arginyl transferase (ATE1). This provides molecular evidence of N-terminal Cys-sulfinic acid formation and arginylation by N-end rule pathway components, and a substrate of ATE1 in plants. PCOs catalyse dioxygenation of the ERF-VII peptides RAP2_2 to RAP2_11
physiological function
PCO dioxygenase activity produces Cys-sulfinic acid at the N-terminus of an ERF-VII peptide, which then undergoes efficient arginylation by an arginyl transferase (ATE1). This provides molecular evidence of N-terminal Cys-sulfinic acid formation and arginylation by N-end rule pathway components, and a substrate of ATE1 in plants. Proposed arginylation requirements for the Arg/Cys branch of the N-end rule pathway
physiological function
regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu, or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation. In plants, ATE is not required for viability. The arginylation branch of the N-end rule pathway is also responsible for repressing expression of the meristempromoting brevipedicellus (BP) gene during leaf development, acting in a redundant way with the asymmetric leaves 1 (AS1) transcription factor complex, a known negative regulator of BP expression
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ATE1_ARATH
632
0
71541
Swiss-Prot
other Location (Reliability: 4)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
generation of RAP2.12 stabilization in ate1 ate2 double-null mutant plant lines
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged enzyme ATE1 from Escherichia coli strain BL21-CodonPlus (DE3)-RIL by nickel affinity chromatography, tag cleavage by TEV protease, and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ATE1 or At5g05700, sequence comparisons, phylogenetic analysis and domain location of ATE protein sequences among plant species
gene ATE1, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIL
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
plant cysteine oxidases (PCOs) and enzyme ATE1 may be viable intervention targets to stabilize N-end rule substrates, including ERF-VIIs, to enhance submergence tolerance in agriculture
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoshida, S.; Ito, M.; Callis, J.; Nishida, I.; Watanabe, A.
A delayed leaf senescence mutant is defective in arginyl-tRNA: protein arginyltransferase, a component of the N-end rule pathway in Arabidopsis
Plant J.
32
129-137
2002
Arabidopsis thaliana
Holman, T.J.; Jones, P.D.; Russell, L.; Medhurst, A.; Ubeda Tomas, S.; Talloji, P.; Marquez, J.; Schmuths, H.; Tung, S.A.; Taylor, I.; Footitt, S.; Bachmair, A.; Theodoulou, F.L.; Holdsworth, M.J.
The N-end rule pathway promotes seed germination and establishment through removal of ABA sensitivity in Arabidopsis
Proc. Natl. Acad. Sci. USA
106
4549-4554
2009
Arabidopsis thaliana (Q9ZT48), Arabidopsis thaliana
Domitrovic, T.; Fausto, A.; Silva, T.; Romanel, E.; Vaslin, M.
Plant arginyltransferases (ATEs)
Genet. Mol. Biol.
40
253-260
2017
Arabidopsis thaliana (Q9ZT48), Chlamydomonas reinhardtii (A0A2K3D0B7), Oryza sativa Japonica Group (Q688J5), Physcomitrium patens (A0A2K1KVV8), Populus trichocarpa (A0A2K1YWL5), Sorghum bicolor (C5YYU0), Vitis vinifera (A0A438HA55)
White, M.D.; Klecker, M.; Hopkinson, R.J.; Weits, D.A.; Mueller, C.; Naumann, C.; O'Neill, R.; Wickens, J.; Yang, J.; Brooks-Bartlett, J.C.; Garman, E.F.; Grossmann, T.N.; Dissmeyer, N.; Flashman, E.
Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets
Nat. Commun.
8
14690
2017
Arabidopsis thaliana (Q9ZT48)
EXTERNAL LINKS (specific for EC-Number 2.3.2.8)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
