The structure of Arabidopsis phytochrome A reveals topological and functional diversification among the plant photoreceptor isoforms.

The structure of Arabidopsis phytochrome A reveals topological and functional diversification among the plant photoreceptor isoforms.
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DOI:
10.1038/s41477-023-01435-8
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发表时间:
2023-07
期刊:
影响因子:
18
通讯作者:
Li, Huilin
Li, Huilin
中科院分区:
生物学1区
文献类型:
--
作者:
Burgie, E. Sethe;Li, Hua;Gannam, Zachary T. K.;McLoughlin, Katrice E.;Vierstra, Richard D.;Li, Huilin

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植物利用不同的光敏色素 (Phy) 光感受器群,通过非活性 Pr 和活性 Pfr 构象异构体之间的可逆光互变来控制形态发生的许多方面。两个最有影响力的是 PhyA,其保留 Pfr 可以感知微弱的光,而 PhyB 的 Pfr 相对不稳定,使其更适合检测全日照和温度。为了更好地理解这些对比,我们通过冷冻电子显微镜解析了全长 PhyA 作为 Pr 的三维结构。与 PhyB 一样,PhyA 通过其 C 端组氨酸激酶相关结构域 (HKRD) 的头对头组装来二聚化,而其余部分则组装为头对尾光响应平台。尽管平台和 HKRD 在 PhyB 二聚体中不对称连接,但这些不对称连接在 PhyA 中不存在。对截短和定点突变体的分析表明,这种解耦和改变的平台组装对 PhyA 的 Pfr 稳定性具有功能性影响,并强调了植物 Phy 结构多样化如何扩展光和温度感知。
Plants employ a divergent cohort of phytochrome (Phy) photoreceptors to govern many aspects of morphogenesis through reversible photointerconversion between inactive Pr and active Pfr conformers. The two most influential are PhyA whose retention of Pfr enables sensation of dim light, while the relative instability of Pfr for PhyB makes it better suited for detecting full sun and temperature. To better understand these contrasts, we solved, by cryo-electron microscopy, the three-dimensional structure of full-length PhyA as Pr. Like PhyB, PhyA dimerizes through head-to-head assembly of its C-terminal histidine kinase-related domains (HKRDs), while the remainder assembles as a head-to-tail light-responsive platform. Whereas the platform and HKRDs associate asymmetrically in PhyB dimers, these lopsided connections are absent in PhyA. Analysis of truncation and site-directed mutants revealed that this decoupling and altered platform assembly have functional consequences for Pfr stability of PhyA and highlights how plant Phy structural diversification has extended light and temperature perception.
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