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Triple loss of function of protein phosphatases type 2C leads to partial constitutive response to endogenous abscisic acid.2C型蛋白磷酸酶的三重功能丧失导致对内源脱落酸的部分组成型反应。
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Regulators of PP2C phosphatase activity function as abscisic acid sensors.PP2C磷酸酶活性调节剂作为脱落酸传感器发挥作用。
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Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins.脱落酸通过START蛋白的PYR/PYL家族抑制2C型蛋白磷酸酶。
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二聚体 PYR1 结合和信号转导的脱落酸结构机制。

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

机构信息

Division of Biological Sciences, Cell and Developmental Biology Section, University of California at San Diego, La Jolla, CA 92093, USA.

出版信息

Science. 2009 Dec 4;326(5958):1373-9. doi: 10.1126/science.1181829. Epub 2009 Oct 22.

DOI:10.1126/science.1181829
PMID:19933100
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2835493/
Abstract

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.

摘要

植物激素脱落酸（ABA）在种子休眠、植物发育、耐旱性和对环境胁迫的适应反应中发挥作用。介导 ABA 受体识别和信号转导的结构机制尚不清楚，但对于理解和操纵非生物胁迫抗性至关重要。在这里，我们报告了 pyrabactin 抗性 1（PYR1）的结构，PYR1 是典型的 PYR/PYR1 样（PYL）/ABA 受体（RCAR）蛋白的调节成分，在早期 ABA 信号转导中发挥作用。晶体结构揭示了一个 α/β 螺旋夹折叠和同源二聚体组装，通过共免疫沉淀在体内得到验证。ABA 在一个大的内部腔中的结合将结构基序从无 ABA 的“开 lid”转换为 ABA 结合的“闭 lid”构象。小角度 X 射线散射表明，ABA 通过将 PYR1 转换为更紧凑、对称的闭合 lid 二聚体来传递信号。设计用于破坏激素结合的定点突变 PYR1 会失去在植物体内与 2C 型蛋白磷酸酶伙伴的 ABA 触发相互作用。