@article{oai:repo.qst.go.jp:00079901,
 author = {Takehara, Sayaka and Sakuraba, Shun and Mikami, Bunzo and Yoshida, Hideki and Yoshimura, Hisako and Itho, Aya and Endo, Masaki and Watanabe, Nobuhisa and Nagae, Takayuki and Matsuoka, Makoto and Miyako, Ueguchi-Tanaka and Sakuraba, Shun},
 journal = {Nature communications},
 month = {May},
 note = {X-ray structural analysis of gibberellin (GA) and auxin inactivation enzymes GA 2-oxidase 3 (GA2ox3) and auxin dioxygenase was used to elucidate the post-translational regulatory mechanism of homeostasis of growth phytohormones in rice. Results revealed that both enzymes form multimers by bridging their substrates, GA4 and indole acetic acid (IAA), at their interface regions. Further functional analyses revealed that multimerization of these enzymes gradually proceeds with increasing GA4 and IAA concentrations, and multimerized enzymes have much higher specific activities than monomer forms, a system that should favour homeostasis maintenance of these phytohormones. Molecular dynamic analysis explained the mechanism responsible for increasing GA2ox3 activity by multimerization—GA4 in the interface of oligomerized GA2ox3s can enter the active site with a low energy barrier. In summary, we report that the homeostatic systems for maintaining GA and IAA levels, based on the same allosteric mechanism, developed independently at the times when seed plants and angiosperms appeared.},
 title = {A common allosteric mechanism regulates homeostatic inactivation of auxin and gibberellin},
 volume = {11},
 year = {2020}
}