المؤلفون: Valérie Nicolas-Francès, Jordan Rossi, Claire Rosnoblet, Carole Pichereaux, Siham Hichami, Jeremy Astier, Agnès Klinguer, David Wendehenne, Angélique Besson-Bard

المصدر: Frontiers in Plant Science, Vol 13 (2022)

مصطلحات موضوعية: Arabidopsis thaliana, protein tyrosine phosphatase 1, nitric oxide, S-nitrosation, H2O2, oxidation, Plant culture, SB1-1110

الوصف: 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.

وصف الملف: electronic resource

العلاقة: https://www.frontiersin.org/articles/10.3389/fpls.2022.807249/fullTest; https://doaj.org/toc/1664-462XTest

الوصول الحر: https://doaj.org/article/0daf20613ef540b69695c96fae899ca9Test

المؤلفون: Valérie Nicolas-Francès, Jordan Rossi, Claire Rosnoblet, Carole Pichereaux, Siham Hichami, Jeremy Astier, Agnès Klinguer, David Wendehenne, Angélique Besson-Bard

مصطلحات موضوعية: Botany, Plant Biology, Plant Systematics and Taxonomy, Plant Cell and Molecular Biology, Plant Developmental and Reproductive Biology, Plant Pathology, Plant Physiology, Plant Biology not elsewhere classified, Arabidopsis thaliana, protein tyrosine phosphatase 1, nitric oxide, S-nitrosation, H2O2, oxidation, post-translational modifications, mitogen-activated protein kinases

الوصف: 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 H 2 O 2 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 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 AtPTP1 protein from its irreversible oxidation by H 2 O 2 . This mechanism of protection could be a conserved mechanism in plant PTPases.

العلاقة: https://figshare.com/articles/figure/Image_1_S-Nitrosation_of_Arabidopsis_thaliana_Protein_Tyrosine_Phosphatase_1_Prevents_Its_Irreversible_Oxidation_by_Hydrogen_Peroxide_tif/19152416Test

الإتاحة: https://doi.org/10.3389/fpls.2022.807249.s001Test
https://figshare.com/articles/figure/Image_1_S-Nitrosation_of_Arabidopsis_thaliana_Protein_Tyrosine_Phosphatase_1_Prevents_Its_Irreversible_Oxidation_by_Hydrogen_Peroxide_tif/19152416Test