Thiol-based Oxidative Posttranslational Modifications (OxiPTMs) of Plant Proteins. (22nd March 2022)

• Record Type: Journal Article
• Authors: Corpas, Francisco J; González-Gordo, Salvador; Rodríguez-Ruiz, Marta; Muñoz-Vargas, María A; Palma, José M
• Is Part Of: Plant & cell physiology. Volume 63:Number 7(2022)
• Page Start: 889
• Page End: 900
• Publication Date: 2022-03-22
• Subjects: Persulfidation -- S-cyanylation and S-acylation -- S-glutathionylation -- S-nitrosation -- S-sulfenylation; Plant physiology -- Periodicals; Microbiology -- Periodicals; Cytology -- Periodicals; Cell Physiology -- Periodicals; Plant Physiological Phenomena -- Periodicals; Cytology; Microbiology; Plant physiology; Periodicals; 571.205
• DOI: 10.1093/pcp/pcac036
• Languages: English
• ISSNs: 0032-0781

Abstract

Abstract: The 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.