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Title

Thiol-based oxidative posttranslational modifications (OxiPTMs) of plant proteins

AuthorsCorpas, Francisco J. CSIC ORCID; González-Gordo, Salvador CSIC ORCID; Rodríguez-Ruiz, Marta CSIC ORCID; Muñoz-Vargas, María A. CSIC ORCID; Palma Martínez, José Manuel CSIC ORCID
KeywordsPersulfidation
S-cyanylation and S-acylation
S-glutathionylation
S-nitrosation
S-sulfenylation
Issue Date2022
PublisherOxford University Press
CitationPlant and Cell Physiology 63: 889-900 (2022)
AbstractThe thiol group of cysteine (Cys) residues, often present in the active center of the protein, is of particular importance to protein function, which is significantly determined by the redox state of a protein's environment. Our knowledge of different thiol-based oxidative posttranslational modifications (oxiPTMs), which compete for specific protein thiol groups, has increased over the last 10 years. The principal oxiPTMs include S-sulfenylation, S-glutathionylation, S-nitrosation, persulfidation, S-cyanylation and S-acylation. The role of each oxiPTM depends on the redox cellular state, which in turn depends on cellular homeostasis under either optimal or stressful conditions. Under such conditions, the metabolism of molecules such as glutathione, NADPH (reduced nicotinamide adenine dinucleotide phosphate), nitric oxide, hydrogen sulfide and hydrogen peroxide can be altered, exacerbated and, consequently, outside the cell's control. This review provides a broad overview of these oxiPTMs under physiological and unfavorable conditions, which can regulate the function of target proteins.
Publisher version (URL)http://dx.doi.org/10.1093/pcp/pcac036
URIhttp://hdl.handle.net/10261/307493
DOI10.1093/pcp/pcac036
Identifiersdoi: 10.1093/pcp/pcac036
issn: 1471-9053
Appears in Collections:(EEZ) Artículos




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