Protein Persulfidation in Plants: Function and Mechanism

Abstract

As an endogenous gaseous transmitter, the function of hydrogen sulfide (H2S) has been extensively studied in plants. Once synthesized, H2S may be involved in almost all life processes of plants. Among them, a key route for H2S bioactivity occurs via protein persulfidation, in which process oxidizes cysteine thiol (R-SH) groups into persulfide (R-SSH) groups. This process is thought to underpin a myriad of cellular processes in plants linked to growth, development, stress responses, and phytohormone signaling. Multiple lines of emerging evidence suggest that this redox-based reversible post-translational modification can not only serve as a protective mechanism for H2S in oxidative stress, but also control a variety of biochemical processes through the allosteric effect of proteins. Here, we collate emerging evidence showing that H2S-mediated persulfidation modification involves some important biochemical processes such as growth and development, oxidative stress, phytohormone and autophagy. Additionally, the interaction between persulfidation and S-nitrosylation is also discussed. In this work, we provide beneficial clues for further exploration of the molecular mechanism and function of protein persulfidation in plants in the future.

Redox regulation of enzymes involved in sulfate assimilation and in the synthesis of sulfur-containing amino acids and glutathione in plants

“…Hence, persulfidation may represent a protective mechanism operating during oxidative stress conditions. Alternatively, it may constitute a regulatory mechanism that would help controlling protein function/activities in order to adjust the plant response to sulfate availability in case of oxidative stress ( Wang et al, 2021 ). Incidentally, sulfide would be restituted upon persulfide reduction by a dithiol reductant.…”

Biological Functions of Hydrogen Sulfide in Plants

“…The occurrence of H 2 S-mediated S -sulfhydration may be predicated on S -sulfenylation [ 19 , 236 ]. H 2 S finds it difficult to directly reduce the disulfide bonds inside the protein-forming S-sulfide, from the thermodynamic and kinetic points of view [ 247 ].…”

“…On the other hand, H 2 S is involved in the defense mechanisms of plants against various abiotic stresses, including osmotic stress [ 13 ], drought stress [ 14 ], salt stress [ 15 ], extremely high- or low-temperature stress [ 16 ], and metalloids stress [ 17 ], by reducing reactive oxygen species (ROS) accumulation and actively mobilizing bioactive proteins, such as post-translational modification (PTM), as represented by S -sulfhydration [ 18 , 19 ]. H 2 S is capable of interacting with many plant hormones, such as abscisic acid (ABA) [ 20 ], auxin (AUX) [ 21 ], gibberellins (GAs) [ 22 ], ethylene (ETH) [ 6 ], salicylic acid (SA) [ 23 ], jasmonic acid (JA) [ 24 ], and brassinosteroids [ 25 ].…”

N-Acetylcysteine (NAC) and its Immunomodulatory Properties

“…The first hypothesis is based on the observation that many intracellular proteins are persulfidated on cysteine residues, particularly when under oxidative stress. Persulfidation refers to the reversible post-translational modification of protein cysteine thiol (R-SH) groups into persulfide (R-SSH) groups (Wang et al, 2021). Persulfidation is thought to functionally modulate proteins in order to adapt metabolism and signal transduction to conditions of oxidative stress (Pedre et al, 2021).…”