How Does the Ribosome Fold the Proteome?

IF 12.1 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY Annual review of biochemistry Pub Date : 2020-06-20 DOI:10.1146/annurev-biochem-062917-012226
Anaïs M E Cassaignau, Lisa D Cabrita, John Christodoulou
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引用次数: 36

Abstract

Folding of polypeptides begins during their synthesis on ribosomes. This process has evolved as a means for the cell to maintain proteostasis, by mitigating the risk of protein misfolding and aggregation. The capacity to now depict this cellular feat at increasingly higher resolution is providing insight into the mechanistic determinants that promote successful folding. Emerging from these studies is the intimate interplay between protein translation and folding, and within this the ribosome particle is the key player. Its unique structural properties provide a specialized scaffold against which nascent polypeptides can begin to form structure in a highly coordinated, co-translational manner. Here, we examine how, as a macromolecular machine, the ribosome modulates the intrinsic dynamic properties of emerging nascent polypeptide chains and guides them toward their biologically active structures.

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核糖体如何折叠蛋白质组?
多肽的折叠开始于它们在核糖体上的合成。这一过程已经演变为细胞维持蛋白质稳态的一种手段,通过降低蛋白质错误折叠和聚集的风险。现在以越来越高的分辨率描绘这种细胞壮举的能力,为促进成功折叠的机制决定因素提供了见解。这些研究揭示了蛋白质翻译和折叠之间的密切相互作用,而核糖体颗粒在其中起着关键作用。其独特的结构特性提供了一个专门的支架,新生多肽可以开始以高度协调,共翻译的方式形成结构。在这里,我们研究了作为一个大分子机器,核糖体如何调节新生多肽链的内在动态特性,并引导它们走向其生物活性结构。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Annual review of biochemistry
Annual review of biochemistry 生物-生化与分子生物学
CiteScore
33.90
自引率
0.00%
发文量
31
期刊介绍: The Annual Review of Biochemistry, in publication since 1932, sets the standard for review articles in biological chemistry and molecular biology. Since its inception, these volumes have served as an indispensable resource for both the practicing biochemist and students of biochemistry.
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