Structural basis of abscisic acid signalling

被引：449

作者：

Miyazono, Ken-ichi ^{[1
]}

Miyakawa, Takuya ^{[1
]}

Sawano, Yoriko ^{[1
]}

Kubota, Keiko ^{[1
]}

Kang, Hee-Jin ^{[1
]}

Asano, Atsuko ^{[1
]}

Miyauchi, Yumiko ^{[1
]}

Takahashi, Mihoko ^{[1
]}

Zhi, Yuehua ^{[1
]}

Fujita, Yasunari ^{[2
]}

Yoshida, Takuya ^{[2
,3
]}

Kodaira, Ken-Suke ^{[2
,3
]}

Yamaguchi-Shinozaki, Kazuko ^{[2
,3
]}

Tanokura, Masaru ^{[1
]}

机构：

[1] Univ Tokyo, Grad Sch Agr & Life Sci, Dept Appl Biol Chem, Tokyo 1138657, Japan

[2] Japan Int Res Ctr Agr Sci, Biol Resources Div, Tsukuba 3058686, Japan

[3] Univ Tokyo, Grad Sch Agr & Life Sci, Lab Plant Mol Physiol, Tokyo 1138657, Japan

来源：

NATURE | 2009年 / 462卷 / 7273期

关键词：

PROTEIN-KINASES; STRESS; IDENTIFICATION; TRANSDUCTION; CALMODULIN; FAMILY; GROWTH;

D O I：

10.1038/nature08583

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：609 / U79

页数：7

共 29 条

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