Molecular Microbiology, Department of Biology, University of Konstanz, 78457 Konstanz, Germany.
Trends Biochem Sci. 2012 Jul;37(7):274-83. doi: 10.1016/j.tibs.2012.03.002. Epub 2012 Apr 13.
De novo protein folding is delicate and error-prone and requires the guidance of molecular chaperones. Besides cytosolic and organelle-specific chaperones, cells have evolved ribosome-associated chaperones that support early folding events and prevent misfolding and aggregation. This class of chaperones includes the bacterial trigger factor (TF), the archaeal and eukaryotic nascent polypeptide-associated complex (NAC) and specialized eukaryotic heat shock protein (Hsp) 70/40 chaperones. This review focuses on the cellular activities of ribosome-associated chaperones and highlights new findings indicating additional functions beyond de novo folding. These activities include the assembly of oligomeric complexes, such as ribosomes, modulation of translation and targeting of proteins.
从头折叠蛋白质既精细又容易出错，需要分子伴侣的指导。除了细胞质和细胞器特异性伴侣外，细胞还进化出了核糖体相关伴侣，它们支持早期折叠事件，防止错误折叠和聚集。这类伴侣包括细菌触发因子 (TF)、古菌和真核新生多肽相关复合物 (NAC) 和专门的真核热休克蛋白 (Hsp) 70/40 伴侣。本文重点介绍了核糖体相关伴侣的细胞活性，并强调了新的发现，表明其具有超越从头折叠的额外功能。这些活性包括寡聚复合物的组装，如核糖体，翻译的调节和蛋白质的靶向。
