The <i>Modus Operandi</i> of Hydrogen Sulfide(H<sub>2</sub>S)-Dependent Protein Persulfidation in Higher Plants
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 tech...
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MDPI AG
2021-10-01
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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 |
collection | DOAJ |
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. |
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issn | 2076-3921 |
language | English |
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series | Antioxidants |
spelling | doaj.art-0cf1126c76d0408499d8f8990ca69ae22023-11-22T22:12:12ZengMDPI AGAntioxidants2076-39212021-10-011011168610.3390/antiox10111686The <i>Modus Operandi</i> of Hydrogen Sulfide(H<sub>2</sub>S)-Dependent Protein Persulfidation in Higher PlantsFrancisco J. Corpas0Salvador González-Gordo1María A. Muñoz-Vargas2Marta Rodríguez-Ruiz3José M. Palma4Group of Antioxidants, Free Radicals, and Nitric Oxide in Biotechnology, Food and Agriculture, Department of Biochemistry, Cell and Molecular Biology of Plants, Estación Experimental del Zaidín, Spanish National Research Council, CSIC, C/Profesor Albareda, 1, 18008 Granada, SpainGroup of Antioxidants, Free Radicals, and Nitric Oxide in Biotechnology, Food and Agriculture, Department of Biochemistry, Cell and Molecular Biology of Plants, Estación Experimental del Zaidín, Spanish National Research Council, CSIC, C/Profesor Albareda, 1, 18008 Granada, SpainGroup of Antioxidants, Free Radicals, and Nitric Oxide in Biotechnology, Food and Agriculture, Department of Biochemistry, Cell and Molecular Biology of Plants, Estación Experimental del Zaidín, Spanish National Research Council, CSIC, C/Profesor Albareda, 1, 18008 Granada, SpainGroup of Antioxidants, Free Radicals, and Nitric Oxide in Biotechnology, Food and Agriculture, Department of Biochemistry, Cell and Molecular Biology of Plants, Estación Experimental del Zaidín, Spanish National Research Council, CSIC, C/Profesor Albareda, 1, 18008 Granada, SpainGroup of Antioxidants, Free Radicals, and Nitric Oxide in Biotechnology, Food and Agriculture, Department of Biochemistry, Cell and Molecular Biology of Plants, Estación Experimental del Zaidín, Spanish National Research Council, CSIC, C/Profesor Albareda, 1, 18008 Granada, SpainProtein 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.https://www.mdpi.com/2076-3921/10/11/1686hydrogen sulfidepersulfidationoxidative posttranslational modifications<i>S</i>-desulfurization |
spellingShingle | 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 Antioxidants hydrogen sulfide persulfidation oxidative posttranslational modifications <i>S</i>-desulfurization |
title | 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_short | 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 |
topic | hydrogen sulfide persulfidation oxidative posttranslational modifications <i>S</i>-desulfurization |
url | https://www.mdpi.com/2076-3921/10/11/1686 |
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