Abstract
Hydrogen sulfide (H2S) has been largely referred as a toxic gas and environmental hazard, but recent years, it has emerged as an important gas-signaling molecule with effects on multiple physiological processes in both animal and plant systems. The regulatory functions of H2S in plants are involved in important processes such as the modulation of defense responses, plant growth and development, and the regulation of senescence and maturation. The main signaling pathway involving sulfide has been proven to be through protein persulfidation (alternatively called S-sulfhydration), in which the thiol group of cysteine (-SH) in proteins is modified into a persulfide group (-SSH). This modification may cause functional changes in protein activities, structures, and subcellular localizations of the target proteins. New shotgun proteomic approaches and bioinformatic analyses have revealed that persulfidated cysteines regulate important biological processes, highlighting their importance in cell signaling, since about one in 20 proteins in Arabidopsis is persulfidated. During oxidative stress, an increased persulfidation has been reported and speculated that persulfidation is the protective mechanism for protein oxidative damage. Nevertheless, cysteine residues are also oxidized to different post-translational modifications such S-nitrosylation or S-sulfenylation, which seems to be interconvertible. Thus, it must imply a tight cysteine redox regulation essential for cell survival. This review is aimed to focus on the current knowledge of protein persulfidation and addresses the regulation mechanisms that are disclosed based on the knowledge from other cysteine modifications.
Highlights
Hydrogen sulfide (H2S) is an inorganic, flammable, water-soluble gas with a noticeable odor of rotten eggs
Numerous reports highlight the importance of H2S as a signaling molecule, its primary mechanism of action has been recently deciphered (Mustafa et al, 2009; Aroca et al, 2015). It has been explained through a new post-translational modification (PTM) of proteins, named persulfidation, where reactive cysteine residues on target proteins are modified via conversion of the thiol group (-SH) into a persulfide group (-SSH)
This study revealed that 2,015 proteins (5% of the Arabidopsis proteome) were modified by persulfidation and that approximately 3,200 proteins were potentially targets for this modification in mature plants
Summary
Hydrogen sulfide (H2S) is an inorganic, flammable, water-soluble gas with a noticeable odor of rotten eggs. In the past decade, it has emerged as a new gaseous signaling molecule (gasotransmitter) in animal and plant cells and is as important as nitric oxide (NO), carbon monoxide (CO), and hydrogen peroxide (H2O2) (Garcia-Mata and Lamattina, 2010; Vandiver and Snyder, 2012; Kimura, 2014). Since 1996, when H2S was first described as an endogenous neuromodulator in animals (Abe and Kimura, 1996), an increasing number of articles have described its physiological effects on plants and animals. H2S is involved in many physiological and pathological processes in animals, such as apoptosis, inflammatory processes, the protective effects against hypoxia, neuromodulation, cell proliferation and cardioprotection, among others, as described in several recent reports and reviews (Wang, 2014; Olas, 2015; Paul and Snyder, 2015a)
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