A common allosteric mechanism regulates homeostatic inactivation of auxin and gibberellin

Abstract

Allosteric regulation is protein activation by effector binding at a site other than the active site. Here, we show via X-ray structural analysis of gibberellin 2-oxidase 3 (GA2ox3), and auxin dioxygenase (DAO), that such a mechanism maintains hormonal homeostasis in plants. Both enzymes form multimers by interacting via GA(4) and indole-3-acetic acid (IAA) at their binding interface. Via further functional analyses we reveal that multimerization of these enzymes gradually proceeds with increasing GA(4) and IAA concentrations; multimerized enzymes have higher specific activities than monomer forms, a system that should favour the maintenance of homeostasis for these phytohormones. Molecular dynamic analysis suggests a possible mechanism underlying increased GA2ox3 activity by multimerization-GA(4) in the interface of oligomerized GA2ox3s may be able to enter the active site with a low energy barrier. In summary, homeostatic systems for maintaining GA and IAA levels, based on a common allosteric mechanism, appear to have developed independently. Enzymatic inactivation of gibberellins and auxin, via GA2ox3 and DAO respectively, contributes to hormone homeostasis in plants. Here Takehara et al. show that both enzymes multimerize in a substrate-concentration-dependent manner, and that this multimerization leads to increased enzyme activity.