Persulfidation-based Modification of Cysteine Desulfhydrase and the NADPH Oxidase RBOHD Controls Guard Cell Abscisic Acid Signaling

编号 040023203

推送时间 20200330

研究领域 森林培育 

年份 2020 

类型 期刊 

语种 英语

标题 Persulfidation-based Modification of Cysteine Desulfhydrase and the NADPH Oxidase RBOHD Controls Guard Cell Abscisic Acid Signaling

来源期刊 The Plant Cell

期 第232期

发表时间 20200220

关键词 Abscisic Acid Signaling;  NADPH oxidase;  Persulfidation;  Guard cells; 

摘要 Accumulating evidence suggests that hydrogen sulfide (H2S) is a gaseous signaling molecule that regulates diverse cellular signaling pathways through persulfidation, which involves the post translational modification (PTM) of specific cysteine residues to form persulfides. However, the mechanisms that underlie this important redox-based PTM remain poorly understood in higher plants. We have, therefore, analyzed how protein persulfidation acts as a specific and reversible signaling mechanism during the plant abscisic acid (ABA) response. Here we show that ABA stimulates the persulfidation of L-cysteine desulfhydrase 1 (DES1), an important endogenous H2S enzyme, at Cys44 and Cys205 in a redox-dependent manner. Moreover, sustainable H2S accumulation drives persulfidation of the NADPH oxidase respiratory burst oxidase homolog protein D (RBOHD) at Cys825 and Cys890, which enhance its ability to produce reactive oxygen species. Physiologically, S-persulfidation-induced RBOHD activity is relevant to ABA-induced stomatal closure. Together, these processes form a negative feedback loop that fine-tunes guard cell redox homeostasis and ABA signaling. These findings not only expand our current knowledge of H2S function in the context of guard cell ABA signaling, but also demonstrate the presence of a rapid signal integration mechanism involving specific and reversible redox-based PTMs that occur in response to changing environmental conditions.

服务人员 孙小满

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