Structural basis of abscisic acid signalling

Ken-ichi Miyazono, Takuya Miyakawa, Yoriko Sawano, Keiko Kubota, Hee-Jin Kang, Atsuko Asano, Yumiko Miyauchi, Mihoko Takahashi, Yuehua Zhi, Yasunari Fujita, Takuya Yoshida, Ken-Suke Kodaira, Kazuko Yamaguchi-Shinozaki and Masaru Tanokura ()
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Ken-ichi Miyazono: Graduate School of Agricultural and Life Sciences, The University of Tokyo
Takuya Miyakawa: Graduate School of Agricultural and Life Sciences, The University of Tokyo
Yoriko Sawano: Graduate School of Agricultural and Life Sciences, The University of Tokyo
Keiko Kubota: Graduate School of Agricultural and Life Sciences, The University of Tokyo
Hee-Jin Kang: Graduate School of Agricultural and Life Sciences, The University of Tokyo
Atsuko Asano: Graduate School of Agricultural and Life Sciences, The University of Tokyo
Yumiko Miyauchi: Graduate School of Agricultural and Life Sciences, The University of Tokyo
Mihoko Takahashi: Graduate School of Agricultural and Life Sciences, The University of Tokyo
Yuehua Zhi: Graduate School of Agricultural and Life Sciences, The University of Tokyo
Yasunari Fujita: Japan International Research Center for Agricultural Sciences
Takuya Yoshida: Japan International Research Center for Agricultural Sciences
Ken-Suke Kodaira: Japan International Research Center for Agricultural Sciences
Kazuko Yamaguchi-Shinozaki: Japan International Research Center for Agricultural Sciences
Masaru Tanokura: Graduate School of Agricultural and Life Sciences, The University of Tokyo

Nature, 2009, vol. 462, issue 7273, 609-614

Abstract: Abstract The phytohormone abscisic acid (ABA) mediates the adaptation of plants to environmental stresses such as drought and regulates developmental signals such as seed maturation. Within plants, the PYR/PYL/RCAR family of START proteins receives ABA to inhibit the phosphatase activity of the group-A protein phosphatases 2C (PP2Cs), which are major negative regulators in ABA signalling. Here we present the crystal structures of the ABA receptor PYL1 bound with (+)-ABA, and the complex formed by the further binding of (+)-ABA-bound PYL1 with the PP2C protein ABI1. PYL1 binds (+)-ABA using the START-protein-specific ligand-binding site, thereby forming a hydrophobic pocket on the surface of the closed lid. (+)-ABA-bound PYL1 tightly interacts with a PP2C domain of ABI1 by using the hydrophobic pocket to cover the active site of ABI1 like a plug. Our results reveal the structural basis of the mechanism of (+)-ABA-dependent inhibition of ABI1 by PYL1 in ABA signalling.

Date: 2009
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DOI: 10.1038/nature08583

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