Corpas Francisco J, González-Gordo Salvador, Muñoz-Vargas María A, Rodríguez-Ruiz Marta, Palma José M
Group 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, Spain.
Antioxidants (Basel). 2021 Oct 26;10(11):1686. doi: 10.3390/antiox10111686.
Protein persulfidation is a post-translational modification (PTM) mediated by hydrogen sulfide (HS), 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 -nitrosation, glutathionylation, sulfenylation, -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.
蛋白质过硫化是一种由硫化氢（HS）介导的翻译后修饰（PTM），它会影响目标蛋白质中半胱氨酸残基的巯基，并且对蛋白质功能可能产生正向、负向或零影响。由于蛋白质组学技术的进步，在高等植物中鉴定出的受这种PTM影响的潜在蛋白质靶点数量大幅增加。然而，其对生物学功能的确切影响需要在纯化蛋白质的实验水平上进行评估，以确定受影响的特定半胱氨酸残基。鉴于不同的氧化翻译后修饰（oxiPTM）之间的潜在相互作用，如亚硝化、谷胱甘肽化、亚磺酰化、氰化和S-酰化，它们也会影响巯基，因此还需要在细胞氧化还原水平上进行评估。本综述旨在提供关于过硫化在高等植物中发挥的重要生理作用的最新全面概述，过硫化作为一种蛋白质保护免受不可逆氧化的细胞机制。
