Abstract
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 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 S-nitrosation, glutathionylation, sulfenylation, S-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.
Highlights
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S-desulfurization mitigates the inhibition by persulfidation of various enzymes including alliinase, D-lactate dehydrogenase (D-LDH), alcohol dehydrogenase (ADH) and glucose-6-phosphate dehydrogenase (G6PDH) [55]. These findings provide further confirmation of the important role played by persulfidation in the regulation of its target proteins
The important role of Hydrogen sulfide (H2 S) in the physiology of higher plants is widely recognized, with the H2 S-based post-translational modification (PTM) protein persulfidation being effective at modulating the function of target proteins
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. The consensus surrounding the biological function of H2 S was established 25 years ago through Professor Hideo Kimura’s pioneer animal systems research group. They discovered that H2 S is endogenously generated and acts as a brain neuromodulator [1] whereas later was found to regulate smooth muscle tone [2]. It is important to note that the effect of exogenous H2 S in higher plants was explored and reported even before its impact on mammalian cells was described. All these wide spectra of functions exerted by H2 S are done usually in coordination with other molecules with regulatory properties such as nitric oxide, hydrogen peroxide, carbon monoxide, melatonin, abscisic acid, gibberellins, cytokinins, or ethylene. H2 S is endogenously generated in the cellular cysteine metabolism and is no longer regarded by the scientific community as a harmful by-product, but rather as a signal molecule, with the capacity to regulate the cellular metabolism, either by itself or in cooperation with other signal molecules such as nitric oxide (NO) [24,25]
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