期刊
FRONTIERS IN PLANT SCIENCE
卷 13, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fpls.2022.807249
关键词
Arabidopsis thaliana; protein tyrosine phosphatase 1; nitric oxide; S-nitrosation; H2O2; oxidation; post-translational modifications; mitogen-activated protein kinases
资金
- Ministere de l'Enseignement Superieur, de la Recherche et de l'Innovation, Investissements d'Avenir program, project ISITE-BFC NOISELESS [ANR-15-IDEX-0003, NOISELESS-RA18041.AEC.IS]
- Agence Nationale de la Recherche, project ALGAE-NOS [ANR-18-CE20-0022-02]
- Region de Bourgogne, project RHINO [2018Y-07113]
- Agence Nationale de la Recherche (ANR) [ANR-18-CE20-0022] Funding Source: Agence Nationale de la Recherche (ANR)
Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) acts as a repressor of H2O2 production and regulates the activity of MAPKs. Exogenous H2O2 and NO directly inhibit the protein activity of AtPTP1, and the effect of NO is mediated by S-nitrosation, which protects the protein from H2O2-induced oxidation.
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 (AtPTP1), the only Tyr-specific PTPase present in this plant, acts as a repressor of H2O2 production and regulates the activity of MPK3/MPK6 MAPKs by direct dephosphorylation. Here, we report that recombinant histidine (His)-AtPTP1 protein activity is directly inhibited by H2O2 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 AtPTP1 protein from its irreversible oxidation by H2O2. This mechanism of protection could be a conserved mechanism in plant PTPases.
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