Structural mechanism of abscisic acid binding and signaling by dimeric PYR1.

Structural mechanism of abscisic acid binding and signaling by dimeric PYR1.
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DOI:
10.1126/science.1181829
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发表时间:
2009-12-04
期刊:
Science (New York, N.Y.)
影响因子:
--
通讯作者:
Getzoff ED
Getzoff ED
中科院分区:
其他
文献类型:
--
作者:
Nishimura N;Hitomi K;Arvai AS;Rambo RP;Hitomi C;Cutler SR;Schroeder JI;Getzoff ED

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植物激素脱落酸(阿坝)在种子休眠、植物发育、耐旱性和对环境胁迫的适应性反应中起作用。介导阿坝受体识别和信号传导的结构机制仍然未知,但对于理解和操纵非生物胁迫抗性是必不可少的。在这里,我们报告PYR 1,一个原型PYR/PYL/RCAR蛋白,在早期阿坝信号传导的功能结构。晶体学结构显示α/β螺旋夹折叠和同源二聚体组装,通过免疫共沉淀在体内验证。阿坝结合在一个大的内部空腔开关的结构图案区分ABA-自由的“开盖”从ABA结合的“闭盖”构象。小角X-射线散射表明,阿坝信号转换PYR 1到一个更紧凑,对称的闭盖二聚体。定点PYR 1突变体设计破坏激素结合失去ABA触发的相互作用与2C型蛋白磷酸酶合作伙伴在植物。
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 PYR1, a prototypical PYR/PYL/RCAR protein that functions in early ABA signaling. The crystallographic structure reveals an α/β helix-grip fold and homodimeric assembly, verified in vivo by co-immunoprecipitation. 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.
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