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酵母朊病毒变异性的结构基础。

Structural Bases of Prion Variation in Yeast.

机构信息

A.N. Bach Institute of Biochemistry, Federal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Moscow 119071, Russia.

出版信息

Int J Mol Sci. 2022 May 20;23(10):5738. doi: 10.3390/ijms23105738.

Abstract

Amyloids are protein aggregates with a specific filamentous structure that are related to a number of human diseases, and also to some important physiological processes in animals and other kingdoms of life. Amyloids in yeast can stably propagate as heritable units, prions. Yeast prions are of interest both on their own and as a model for amyloids and prions in general. In this review, we consider the structure of yeast prions and its variation, how such structures determine the balance of aggregated and soluble prion protein through interaction with chaperones and how the aggregated state affects the non-prion functions of these proteins.

摘要

淀粉样蛋白是具有特定丝状结构的蛋白质聚集物,与许多人类疾病以及动物和其他生命领域的一些重要生理过程有关。酵母中的淀粉样蛋白可以稳定地作为可遗传的单位传播,即朊病毒。酵母朊病毒本身以及作为一般淀粉样蛋白和朊病毒的模型都具有重要的研究意义。在这篇综述中,我们考虑了酵母朊病毒的结构及其变化,这些结构如何通过与伴侣蛋白的相互作用来决定聚集态和可溶性朊病毒蛋白之间的平衡,以及聚集态如何影响这些蛋白质的非朊病毒功能。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/af79/9147965/81ebaa2a8dc3/ijms-23-05738-g001.jpg

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