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Interactions between the ACT Domains and Catalytic Subunits of Acetohydroxyacid Synthases (AHASs) from Different
Yonghui Xie1, Xin Wen1, Dongmei Zhao1
1State Key Laboratory of Elemento-Organic Chemistry, Department of Chemical Biology, National Pesticide Engineering Research Center (Tianjin), Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), College of Chemistry, Nankai University, Tianjin, 300071, P.R. China.
Abstract:
Acetohydroxyacid synthase (AHAS), which catalyzes the first step in the biosynthesis of branched-chain amino acids, is a target of several types of potent herbicides and antimicrobials. AHAS contains the catalytic subunit (CS) and the regulatory subunit (RS). The AHAS RS is usually composed of ACT domains and C-terminal domains. Herein, it is reported that the ACT domain of AHAS RS from different species could efficiently activate its respective CS. Moreover, the universal cross-activation between the CSs and the ACT domains of RSs across species has been discovered. Based on these biochemical and structural analyses, a molecular basis for the universal ACT-triggered CS activation is proposed, which would help to design broad-spectrum herbicides by targeting the interaction interface between CS and ACT from different species.
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