The Modus Operandi of Hydrogen Sulfide(H2S)-Dependent Protein Persulfidation in Higher Plants

Protein persulfidation is a post-translational modification (PTM) mediated by hydrogen sulfide (H2S), which affects the thiol group of cysteine residues from target proteins and can have a positive, negative or zero impact on protein function. Due to advances in proteomic tech...

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Autores principales:	Francisco J. Corpas, Salvador González-Gordo, María A. Muñoz-Vargas, Marta Rodríguez-Ruiz, José M. Palma
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	hydrogen sulfide persulfidation oxidative posttranslational modifications <i>S</i>-desulfurization Therapeutics. Pharmacology RM1-950
Acceso en línea:	https://doaj.org/article/0cf1126c76d0408499d8f8990ca69ae2
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spelling	oai:doaj.org-article:0cf1126c76d0408499d8f8990ca69ae22021-11-25T16:26:09ZThe <i>Modus Operandi</i> of Hydrogen Sulfide(H<sub>2</sub>S)-Dependent Protein Persulfidation in Higher Plants10.3390/antiox101116862076-3921https://doaj.org/article/0cf1126c76d0408499d8f8990ca69ae22021-10-01T00:00:00Zhttps://www.mdpi.com/2076-3921/10/11/1686https://doaj.org/toc/2076-3921Protein persulfidation is a post-translational modification (PTM) mediated by hydrogen sulfide (H<sub>2</sub>S), which affects the thiol group of cysteine residues from target proteins and can have a positive, negative or zero impact on protein function. Due to advances in proteomic techniques, the number of potential protein targets identified in higher plants, which are affected by this PTM, has increased considerably. However, its precise impact on biological function needs to be evaluated at the experimental level in purified proteins in order to identify the specific cysteine(s) residue(s) affected. It also needs to be evaluated at the cellular redox level given the potential interactions among different oxidative post-translational modifications (oxiPTMs), such as <i>S</i>-nitrosation, glutathionylation, sulfenylation, <i>S</i>-cyanylation and S-acylation, which also affect thiol groups. This review aims to provide an updated and comprehensive overview of the important physiological role exerted by persulfidation in higher plants, which acts as a cellular mechanism of protein protection against irreversible oxidation.Francisco J. CorpasSalvador González-GordoMaría A. Muñoz-VargasMarta Rodríguez-RuizJosé M. PalmaMDPI AGarticlehydrogen sulfidepersulfidationoxidative posttranslational modifications<i>S</i>-desulfurizationTherapeutics. PharmacologyRM1-950ENAntioxidants, Vol 10, Iss 1686, p 1686 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	hydrogen sulfide persulfidation oxidative posttranslational modifications <i>S</i>-desulfurization Therapeutics. Pharmacology RM1-950
spellingShingle	hydrogen sulfide persulfidation oxidative posttranslational modifications <i>S</i>-desulfurization Therapeutics. Pharmacology RM1-950 Francisco J. Corpas Salvador González-Gordo María A. Muñoz-Vargas Marta Rodríguez-Ruiz José M. Palma The <i>Modus Operandi</i> of Hydrogen Sulfide(H<sub>2</sub>S)-Dependent Protein Persulfidation in Higher Plants
description	Protein persulfidation is a post-translational modification (PTM) mediated by hydrogen sulfide (H<sub>2</sub>S), which affects the thiol group of cysteine residues from target proteins and can have a positive, negative or zero impact on protein function. Due to advances in proteomic techniques, the number of potential protein targets identified in higher plants, which are affected by this PTM, has increased considerably. However, its precise impact on biological function needs to be evaluated at the experimental level in purified proteins in order to identify the specific cysteine(s) residue(s) affected. It also needs to be evaluated at the cellular redox level given the potential interactions among different oxidative post-translational modifications (oxiPTMs), such as <i>S</i>-nitrosation, glutathionylation, sulfenylation, <i>S</i>-cyanylation and S-acylation, which also affect thiol groups. This review aims to provide an updated and comprehensive overview of the important physiological role exerted by persulfidation in higher plants, which acts as a cellular mechanism of protein protection against irreversible oxidation.
format	article
author	Francisco J. Corpas Salvador González-Gordo María A. Muñoz-Vargas Marta Rodríguez-Ruiz José M. Palma
author_facet	Francisco J. Corpas Salvador González-Gordo María A. Muñoz-Vargas Marta Rodríguez-Ruiz José M. Palma
author_sort	Francisco J. Corpas
title	The <i>Modus Operandi</i> of Hydrogen Sulfide(H<sub>2</sub>S)-Dependent Protein Persulfidation in Higher Plants
title_short	The <i>Modus Operandi</i> of Hydrogen Sulfide(H<sub>2</sub>S)-Dependent Protein Persulfidation in Higher Plants
title_full	The <i>Modus Operandi</i> of Hydrogen Sulfide(H<sub>2</sub>S)-Dependent Protein Persulfidation in Higher Plants
title_fullStr	The <i>Modus Operandi</i> of Hydrogen Sulfide(H<sub>2</sub>S)-Dependent Protein Persulfidation in Higher Plants
title_full_unstemmed	The <i>Modus Operandi</i> of Hydrogen Sulfide(H<sub>2</sub>S)-Dependent Protein Persulfidation in Higher Plants
title_sort	<i>modus operandi</i> of hydrogen sulfide(h<sub>2</sub>s)-dependent protein persulfidation in higher plants
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/0cf1126c76d0408499d8f8990ca69ae2
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The <i>Modus Operandi</i> of Hydrogen Sulfide(H<sub>2</sub>S)-Dependent Protein Persulfidation in Higher Plants

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