Conformational Freedom and Topological Confinement of Proteins in Biomolecular Condensates.

Conformational Freedom and Topological Confinement of Proteins in Biomolecular Condensates.
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DOI:
10.1016/j.jmb.2021.167348
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发表时间:
2022-01-15
影响因子:
5.6
通讯作者:
Deniz AA
Deniz AA
中科院分区:
生物学2区
文献类型:
--
作者:
Scholl D;Deniz AA

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生物分子缩合和液-液相分离(LLPS)的出现使我们对细胞和分子生物学的理解变得更加复杂。越来越多的证据表明,冷凝物不仅与生理学有关,而且与人类疾病有关。整个凝结物的宏观和中观表征有助于理解其生物功能和功能障碍。相比之下,迄今为止,缩合物的分子水平表征以及缩合物如何改变构成它们的分子的性质仍然相对较少。在这篇小综述中,我们总结并讨论了最近几项研究的结果,这些研究重点关注蛋白质缩合的结构、动力学和相互作用。他们提供的机械见解帮助我们识别自然的相关属性,科学家可以利用它们来调节凝析油系统的行为。我们还讨论了液滴表面的独特环境,并推测了拓扑约束和物理排斥对冷凝物性质的影响。
The emergence of biomolecular condensation and liquid-liquid phase separation (LLPS) introduces a new layer of complexity into our understanding of cell and molecular biology. Evidence steadily grows indicating that condensates are not only implicated in physiology but also human disease. Macro- and mesoscale characterization of condensates as a whole have been instrumental in understanding their biological functions and dysfunctions. By contrast, the molecular level characterization of condensates and how condensates modify the properties of the molecules that constitute them thus far remain comparably scarce. In this minireview we summarize and discuss the findings of several recent studies that have focused on structure, dynamics, and interactions of proteins undergoing condensation. The mechanistic insights they provide help us identify the relevant properties nature and scientists can leverage to modulate the behavior of condensate systems. We also discuss the unique environment of the droplet surface and speculate on effects of topological constraints and physical exclusion on condensate properties.
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