论文题目：Persulfidation-induced Structural Change of SnRK2.6 Establishes Intramolecular Interaction between Phosphorylation and Persulfidation
论文作者：Sisi Chen, Xiaofeng Wang, Honglei Jia, Fali Li, Ying Ma, Johannes Liesche, Mingzhi Liao, Xueting Ding, Cuixia Liu, Ying Chen, Na Li, Jisheng Li*
气体信号分子硫化氢（Hydrogen sulfide）介导的S-硫巯基化修饰（S-persulfidation）可以改变脱落酸（Abscisic acid）信号通路关键激酶蛋白SnKR2.6的结构，从而提高SnKR2.6转移ATP-γ-phosphate基团的效率，导致激酶活性增强。该研究同时证明，SnKR2.6蛋白关键位点的磷酸化修饰水平可以积极调控硫化氢介导的硫巯基化修饰。该研究提出的蛋白质翻译后修饰互作机制不仅为蛋白质翻译后修饰研究提供新思路，同时也为植物抗旱调控理论依据。
Post-translational modifications (PTMs) regulate the activity of SNF1-RELATED PROTEIN KINASE2.6 (SnRK2.6), including phosphorylation and persulfidation. Here, we report how persulfidations and phosphorylations of SnRK2.6 influence each other. The persulfidation of cysteine C131/C137 altered SnRK2.6 structure, resulted in serine S175 residue more close to aspartic acid D140, who belong to ATP-γ-phosphate proton acceptor may effectively improve the transfer efficiency of phosphate groups to S175, thus persulfidation enhanced the phosphorylation level of S175.S267 and C137 were predicted to lie in close proximity on the protein surface. The phosphorylation status of S267 positively regulated the persulfidation level at C137. Tests of responses of dephosphorylated and depersulfidated mutants to ABAand 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. Taken together, we propose a mechanistic model in which certain phosphorylations facilitate persulfidation, which changes SnRK2.6 structure and increases its activity.