Annual Review of Biochemistry ( IF 12.1 ) Pub Date : 2020-06-22 , DOI: 10.1146/annurev-biochem-062917-012226 Anaïs M E Cassaignau 1 , Lisa D Cabrita 1 , John Christodoulou 1
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.
中文翻译:
核糖体如何折叠蛋白质组?
多肽的折叠在它们在核糖体上的合成过程中开始。通过降低蛋白质错误折叠和聚集的风险,这一过程已经演变为细胞维持蛋白质稳态的一种手段。现在以越来越高的分辨率描绘这种细胞壮举的能力正在深入了解促进成功折叠的机制决定因素。从这些研究中得出了蛋白质翻译和折叠之间的密切相互作用,其中核糖体颗粒是关键因素。其独特的结构特性提供了一个专门的支架,新生多肽可以在此支架上以高度协调、共翻译的方式开始形成结构。在这里,我们研究如何作为一个大分子机器,