RESUMO
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.