Literature summary for 2.3.2.8 extracted from

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 (2017), Nat. Commun., 8, 14690 .

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Activating Compound

Activating Compound	Comment	Organism	Structure
plant cysteine oxidases	i.e. PCO dioxygenase, dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets	Arabidopsis thaliana

Application

Application	Comment	Organism
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	Arabidopsis thaliana

Cloned(Commentary)

Cloned (Comment)	Organism
gene ATE1, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIL	Arabidopsis thaliana

Protein Variants

Protein Variants	Comment	Organism
additional information	generation of RAP2.12 stabilization in ate1 ate2 double-null mutant plant lines	Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-arginyl-tRNAArg + ERF-VII peptide	Arabidopsis thaliana	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	tRNAArg + L-arginyl-[ERF-VII peptide]	-	?
L-arginyl-tRNAArg + protein	Arabidopsis thaliana	-	tRNAArg + L-arginyl-[protein]	-	?

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q9ZT48	-	-

Purification (Commentary)

Purification (Comment)	Organism
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	Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-arginyl-tRNAArg + 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	Arabidopsis thaliana	tRNAArg + L-arginyl-[ERF-VII peptide]	-	?
L-arginyl-tRNAArg + 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	Arabidopsis thaliana	tRNAArg + L-arginyl-[ERF-VII peptide]	-	?
L-arginyl-tRNAArg + protein	-	Arabidopsis thaliana	tRNAArg + L-arginyl-[protein]	-	?

Synonyms

Synonyms	Comment	Organism
arginyl transferase	-	Arabidopsis thaliana
Ate1	-	Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Arabidopsis thaliana

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Arabidopsis thaliana

General Information

General Information	Comment	Organism
malfunction	RAP2.12 stabilization in ate1 ate2 double-null mutant plant lines implicates ATE1 as an ERF-VII-targeting arginyl transferase in vivo	Arabidopsis thaliana
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	Arabidopsis thaliana
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	Arabidopsis thaliana

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Release 2023.1 (January 2023)