Structural Mechanism of Abscisic Acid Binding and Signaling by Dimeric PYR1

被引:387
作者
Nishimura, Noriyuki [3 ]
Hitomi, Kenichi [1 ,2 ,4 ]
Arvai, Andrew S. [1 ,2 ]
Rambo, Robert P. [4 ]
Hitomi, Chiharu [1 ,2 ]
Cutler, Sean R. [5 ]
Schroeder, Julian I. [3 ]
Getzoff, Elizabeth D. [1 ,2 ]
机构
[1] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA
[2] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA
[3] Univ Calif San Diego, Cell & Dev Biol Sect, Div Biol Sci, La Jolla, CA 92093 USA
[4] Univ Calif Berkeley, Lawrence Berkeley Lab, Div Life Sci, Berkeley, CA 94720 USA
[5] Univ Calif Riverside, Dept Bot & Plant Sci, Ctr Plant Cell Biol, Riverside, CA 92521 USA
基金
美国国家科学基金会;
关键词
PROTEIN PHOSPHATASE 2C; X-RAY; NEGATIVE REGULATOR; GUARD-CELLS; ARABIDOPSIS; ABI1; TRANSDUCTION; GERMINATION; EXPRESSION; UPSTREAM;
D O I
10.1126/science.1181829
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) acts in seed dormancy, plant development, drought tolerance, and adaptive responses to environmental stresses. Structural mechanisms mediating ABA receptor recognition and signaling remain unknown but are essential for understanding and manipulating abiotic stress resistance. Here, we report structures of pyrabactin resistance 1 (PYR1), a prototypical PYR/PYR1-like (PYL)/regulatory component of ABA receptor (RCAR) protein that functions in early ABA signaling. The crystallographic structure reveals an alpha/beta helix-grip fold and homodimeric assembly, verified in vivo by coimmunoprecipitation. ABA binding within a large internal cavity switches structural motifs distinguishing ABA-free "open-lid" from ABA-bound "closed-lid" conformations. Small-angle x-ray scattering suggests that ABA signals by converting PYR1 to a more compact, symmetric closed-lid dimer. Site-directed PYR1 mutants designed to disrupt hormone binding lose ABA-triggered interactions with type 2C protein phosphatase partners in planta.
引用
收藏
页码:1373 / 1379
页数:7
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