The continuous refreshment of the proteome is critical to maintain protein homeostasis and to adapt cells to changing conditions. Thus, de novo protein biogenesis by ribosomes is vitally important to every cellular system. This process is delicate and error-prone and requires, besides cytosolic chaperones, the guidance by a specialized set of molecular chaperones that bind transiently to the translation machinery and the nascent protein to support early folding events and to regulate cotranslational protein transport. These chaperones include the bacterial trigger factor (TF), the archaeal and eukaryotic nascent polypeptide-associated complex (NAC), and the eukaryotic ribosome-associated complex (RAC). This review focuses on the structures, functions, and substrates of these ribosome-associated chaperones and highlights the most recent findings about their potential mechanisms of action.

中文翻译：

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核糖体中的伴侣相互作用。

蛋白质组的持续更新对于维持蛋白质稳态和使细胞适应不断变化的条件至关重要。因此，核糖体从头蛋白质生物合成对每个细胞系统都至关重要。这个过程是微妙且容易出错的，除了细胞质伴侣蛋白之外，还需要一组专门的分子伴侣蛋白的指导，这些分子伴侣蛋白与翻译机制和新生蛋白质瞬时结合，以支持早期折叠事件并调节共翻译蛋白转运。这些分子伴侣包括细菌触发因子 (TF)、古细菌和真核新生多肽相关复合物 (NAC) 和真核核糖体相关复合物 (RAC)。本次审查侧重于结构、功能、