Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities.

Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities.
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DOI:
10.1016/j.str.2012.12.001
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发表时间:
2013-02-05
期刊:
影响因子:
5.7
通讯作者:
Griffin, Patrick R.
Griffin, Patrick R.
中科院分区:
生物学2区
文献类型:
--
作者:
West, Graham M.;Pascal, Bruce D.;Ng, Ley-Moy;Soon, Fen-Fen;Melcher, Karsten;Xu, H. Eric;Chalmers, Michael J.;Griffin, Patrick R.

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植物通过脱落酸(ABA)调控的途径调节生长和响应环境胁迫,因此这些途径是生物学和农业研究的主要兴趣。ABA应答首先由START蛋白受体的PYR/PYL/RCAR类感知。这些ABA激活的受体破坏snf1相关激酶(SnRKs)的磷酸酶抑制,使激酶信号传导。本研究通过氢/氘交换(HDX)质谱分析,深入了解了ABA信号通路中蛋白质的结构机制(ABA受体PYL2、HAB1磷酸酶和两种激酶SnRK2.3和2.6)。在结合伙伴存在的情况下,磷酸酶上的HDX为涉及Trp385“锁定”的受体特异性构象提供了证据,这是信号传导所必需的。此外,激酶活性与更稳定的封闭构象有关。这些基于溶液的研究补充了静态晶体结构,并提供了对ABA信号通路的更详细的了解。
Plants regulate growth and respond to environmental stress through abscisic acid (ABA) regulated pathways, and as such these pathways are of primary interest for biological and agricultural research. The ABA response is first perceived by the PYR/PYL/RCAR class of START protein receptors. These ABA activated receptors disrupt phosphatase inhibition of Snf1-related kinases (SnRKs) enabling kinase signaling. Here, insights into the structural mechanism of proteins in the ABA signaling pathway (the ABA receptor PYL2, HAB1 phosphatase, and two kinases, SnRK2.3 and 2.6) are discerned through hydrogen/deuterium exchange (HDX) mass spectrometry. HDX on the phosphatase in the presence of binding partners provides evidence for receptor-specific conformations involving the Trp385 ‘lock’ that is necessary for signaling. Furthermore, kinase activity is linked to a more stable closed conformation. These solution-based studies complement the static crystal structures and provide a more detailed understanding of the ABA signaling pathway.
脱甲酸受体的激素信号传导的栅极锁锁机制。
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