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蛋白质酪氨酸磷酸酶1的S-亚硝化作用可防止其被过氧化氢不可逆氧化。

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

作者信息

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

机构信息

Agroécologie, CNRS, INRAE, Institut Agro, Université de Bourgogne, Université Bourgogne Franche-Comté, Dijon, France.

Fédération de Recherche (FR3450), Agrobiosciences, Interactions et Biodiversité (FRAIB), CNRS, Toulouse, France.

出版信息

Front Plant Sci. 2022 Feb 11;13:807249. doi: 10.3389/fpls.2022.807249. eCollection 2022.

DOI:10.3389/fpls.2022.807249
PMID:35222471
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8867174/
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. protein tyrosine phosphatase 1 (PTP1), the only Tyr-specific PTPase present in this plant, acts as a repressor of HO production and regulates the activity of MPK3/MPK6 MAPKs by direct dephosphorylation. Here, we report that recombinant histidine (His)-PTP1 protein activity is directly inhibited by HO 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 PTP1 protein from its irreversible oxidation by HO. This mechanism of protection could be a conserved mechanism in plant PTPases.

摘要

酪氨酸特异性蛋白酪氨酸磷酸酶（酪氨酸特异性PTP酶）是关键的信号酶，可催化从靶蛋白上磷酸化的酪氨酸残基上去除磷酸基团。这种翻译后修饰尤其能够在防御反应期间调节丝裂原活化蛋白激酶（MAPK）级联反应。蛋白酪氨酸磷酸酶1（PTP1）是该植物中唯一存在的酪氨酸特异性PTP酶，它作为HO产生的抑制剂，并通过直接去磷酸化来调节MPK3/MPK6 MAPK的活性。在此，我们报道重组组氨酸（His）-PTP1蛋白活性受到HO和一氧化氮（NO）外源处理的直接抑制。NO的作用是通过S-亚硝基化发挥的，即NO与还原型半胱氨酸残基之间形成共价键。这种翻译后修饰作用于催化性半胱氨酸C265，并可保护PTP1蛋白免受HO的不可逆氧化。这种保护机制可能是植物PTP酶中的一种保守机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1ad7/8867174/96d24e50d911/fpls-13-807249-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1ad7/8867174/c05cc5ff5265/fpls-13-807249-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1ad7/8867174/9b5cf23e9561/fpls-13-807249-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1ad7/8867174/bafcbcca22a5/fpls-13-807249-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1ad7/8867174/15df894e95c8/fpls-13-807249-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1ad7/8867174/96d24e50d911/fpls-13-807249-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1ad7/8867174/c05cc5ff5265/fpls-13-807249-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1ad7/8867174/9b5cf23e9561/fpls-13-807249-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1ad7/8867174/bafcbcca22a5/fpls-13-807249-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1ad7/8867174/15df894e95c8/fpls-13-807249-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1ad7/8867174/96d24e50d911/fpls-13-807249-g005.jpg

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