Lighting the way: Recent insights into the structure and regulation of phototropin blue light receptors.

Lighting the way: Recent insights into the structure and regulation of phototropin blue light receptors.
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DOI:
10.1016/j.jbc.2021.100594
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发表时间:
2021-01
期刊:
The Journal of biological chemistry
影响因子:
--
通讯作者:
Gardner KH
Gardner KH
中科院分区:
其他
文献类型:
--
作者:
Hart JE;Gardner KH

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趋光素是一种光激活激酶,对植物生理和许多不同的光遗传学工具至关重要。光促蛋白结合了两个蓝光感应光氧电压(LOV)结构域(LOV1和LOV2)和一个c端丝氨酸/苏氨酸激酶结构域,利用LOV结构域控制激酶的催化活性。虽然对光感知LOV结构域的结构和光化学有很多了解,特别是LOV2结构域的激活如何触发α螺旋的展开,将光信号传递给激酶结构域,但关于光结构和机制仍然存在许多问题。最近的研究通过利用小角度x射线散射(SAXS)和其他生物物理方法研究衣藻和拟南芥的多结构域照片,在解决这些问题方面取得了进展,导致模型中结构域具有扩展的线性排列,调节LOV2结构域与激酶结构域n -叶接触。在这篇综述中,我们讨论了这一点以及其他改进了对光调节的结构和机制理解的进展,以及必须克服的挑战,以获得这些令人兴奋的光感受器的高分辨率结构信息。这些信息对于促进对植物生理学的基本理解至关重要,同时使整个植物和分子水平的工程努力成为可能。
The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired. Phototropins combine two blue-light-sensing Light–Oxygen–Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase. While much is known about the structure and photochemistry of the light-perceiving LOV domains, particularly in how activation of the LOV2 domain triggers the unfolding of alpha helices that communicate the light signal to the kinase domain, many questions about phot structure and mechanism remain. Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe. We discuss this and other advances that have improved structural and mechanistic understanding of phot regulation in this review, along with the challenges that will have to be overcome to obtain high-resolution structural information on these exciting photoreceptors. Such information will be essential to advancing fundamental understanding of plant physiology while enabling engineering efforts at both the whole plant and molecular levels.
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