S-Nitrosation of Arabidopsis thaliana Protein Tyrosine Phosphatase 1 Prevents Its Irreversible Oxidation by Hydrogen Peroxide - INRAE - Institut national de recherche pour l’agriculture, l’alimentation et l’environnement Access content directly
Journal Articles Frontiers in Plant Science Year : 2022

S-Nitrosation of Arabidopsis thaliana Protein Tyrosine Phosphatase 1 Prevents Its Irreversible Oxidation by Hydrogen Peroxide

Valérie Nicolas-Francès
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  • PersonId : 1129953
Carole Pichereaux
Siham Hichami
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  • PersonId : 1129954

Abstract

Tyrosine-specific protein tyrosine phosphatases (Tyr-specific PTPases) are key signaling enzymes catalyzing the removal of the phosphate group from phosphorylated tyrosine residues on target proteins. This post-translational modification notably allows the regulation of mitogen-activated protein kinase (MAPK) cascades during defense reactions. Arabidopsis thaliana protein tyrosine phosphatase 1 ( At PTP1), the only Tyr-specific PTPase present in this plant, acts as a repressor of H 2 O 2 production and regulates the activity of MPK3/MPK6 MAPKs by direct dephosphorylation. Here, we report that recombinant histidine (His)- At PTP1 protein activity is directly inhibited by H 2 O 2 and nitric oxide (NO) exogenous treatments. The effects of NO are exerted by S-nitrosation, i.e., the formation of a covalent bond between NO and a reduced cysteine residue. This post-translational modification targets the catalytic cysteine C265 and could protect the At PTP1 protein from its irreversible oxidation by H 2 O 2 . This mechanism of protection could be a conserved mechanism in plant PTPases.
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hal-03603875 , version 1 (14-09-2023)

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Valérie Nicolas-Francès, Jordan Rossi, Claire Rosnoblet, Carole Pichereaux, Siham Hichami, et al.. S-Nitrosation of Arabidopsis thaliana Protein Tyrosine Phosphatase 1 Prevents Its Irreversible Oxidation by Hydrogen Peroxide. Frontiers in Plant Science, 2022, 13, pp.art. 807249. ⟨10.3389/fpls.2022.807249⟩. ⟨hal-03603875⟩
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