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A Novel Chemical Inhibitor of ABA Signaling Targets All ABA Receptors.

Plant Physiol.2017 Apr;173(4):2356-2369. Epub 2017 Feb 13
Yajin Ye 1 , Lijuan Zhou 1 , Xue Liu 1 , Hao Liu 1 , Deqiang Li 1 , Minjie Cao 1 , Haifeng Chen 1 , Lin Xu 1 , Jian-Kang Zhu 2 , Yang Zhao 2
Yajin Ye 1 , Lijuan Zhou 1 , Xue Liu 1 , Hao Liu 1 , Deqiang Li 1 , Minjie Cao 1 , Haifeng Chen 1 , Lin Xu 1 , Jian-Kang Zhu 2 , Yang Zhao 2
+ et al

[No authors listed]

Author information
  • 1 State Key Laboratory of Microbial Metabolism, Department of Bioinformatics and Biostatistics, College of Life Sciences and Biotechnology, Shanghai Jiaotong University, Shanghai 200032, China (X.L., H.-F.C.).
  • 2 State Key Laboratory of Microbial Metabolism, Department of Bioinformatics and Biostatistics, College of Life Sciences and Biotechnology, Shanghai Jiaotong University, Shanghai 200032, China (X.L., H.-F.C.) zhu132@purdue.edu yangzhaotoronto@sina.com.

摘要


Abscisic acid (ABA), the most important stress-induced phytohormone, regulates seed dormancy, germination, plant senescence, and the abiotic stress response. ABA signaling is repressed by group A type 2C protein phosphatases (PP2Cs), and then ABA binds to its receptor of the ACTIN RESISTANCE1 (PYR1), PYR1-LIKE (PYL), and REGULATORY COMPONENTS OF ABA RECEPTORS (RCAR) family, which, in turn, inhibits PP2Cs and activates downstream ABA signaling. The agonist/antagonist of ABA receptors have the potential to reveal the ABA signaling machinery and to become lead compounds for agrochemicals; however, until now, no broad-spectrum antagonists of ABA receptors blocking all PYR/PYL-PP2C interactions have been identified. Here, using chemical genetics screenings, we identified ABA ANTAGONIST1 (AA1), the first broad-spectrum antagonist of ABA receptors in Arabidopsis (Arabidopsis thaliana). Physiological analyses revealed that AA1 is sufficiently active to block ABA signaling. AA1 interfered with all the PYR/PYL-HAB1 interactions, and the diminished PYR/PYL-HAB1 interactions, in turn, restored the activity of HAB1. AA1 binds to all 13 members. Molecular dockings, the non-AA1-bound PYL2 variant, and competitive binding assays demonstrated that AA1 enters into the ligand-binding pocket of PYL2. Using AA1, we tested the genetic relationships of ABA receptors with other core components of ABA signaling, demonstrating that AA1 is a powerful tool with which to sidestep this genetic redundancy of PYR/PYLs. In addition, the application of AA1 delays leaf senescence. Thus, our study developed an efficient broad-spectrum antagonist of ABA receptors and demonstrated that plant senescence can be chemically controlled through AA1, with a simple and easy-to-synthesize structure, allowing its availability and utility as a chemical probe synthesized in large quantities, indicating its potential application in agriculture.