Persulfidation-induced structural change in SnRK2.6 establishes intramolecular interaction between phosphorylation and persulfidation

• DOI: 10.1016/j.molp.2021.07.002
• Publication Date: 2021-07-06T15:31:44Z
• Authors: Sisi Chen; Xiaofeng Wang; Honglei Jia; Fali Li; Ying Ma; Johannes Liesche; Mingzhi Liao; Xueting Ding; Cuixia Liu; Ying Chen; Na Li; Jisheng Li
• Keywords: Models, Molecular; 0303 health sciences; Arabidopsis Proteins; Protein Conformation; Acclimatization; Arabidopsis; Phosphorus; Droughts; DNA-Binding Proteins; Structure-Activity Relationship; 03 medical and health sciences; Mutation; Phosphorylation; Protein Kinases; Protein Processing, Post-Translational; Sulfur; Protein Binding; Transcription Factors

Post-translational modifications (PTMs), including phosphorylation and persulfidation, regulate the activity of SNF1-RELATED PROTEIN KINASE2.6 (SnRK2.6). Here, we report how persulfidations and phosphorylations of SnRK2.6 influence each other. The persulfidation of cysteine C131/C137 alters SnRK2.6 structure and brings the serine S175 residue closer to the aspartic acid D140 that acts as ATP-γ-phosphate proton acceptor, thereby improving the transfer efficiency of phosphate groups to S175 to enhance the phosphorylation level of S175. Interestingly, we predicted that S267 and C137 were predicted to lie in close proximity on the protein surface and found that the phosphorylation status of S267 positively regulates the persulfidation level at C137. Analyses of the responses of dephosphorylated and depersulfidated mutants to abscisic acid and the H2S-donor NaHS during stomatal closure, water loss, gas exchange, Ca2+ influx, and drought stress revealed that S175/S267-associated phosphorylation and C131/137-associated persulfidation are essential for SnRK2.6 function in vivo. In light of these findings, we propose a mechanistic model in which certain phosphorylations facilitate persulfidation, thereby changing the structure of SnRK2.6 and increasing its activity.