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Chaperone binding at the ribosomal exit tunnel

机译：伴侣结合在核糖体出口隧道

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The exit tunnel region of the ribosome is well established as a focal point for interaction between the components that guide the fate of nascent polypeptides. One of these, the chaperone trigger factor (TF), associates with the 50S ribosomal subunit through its N-terminal domain. Targeting of TF to ribosomes is crucial to achieve its remarkable efficiency in protein folding. A similar tight coupling to translation is found in signal recognition particle (SRP)-dependent protein translocation. Here, we report crystal structures of the E. coli TF ribosome binding domain. TF is structurally related to the Hsp33 chaperone but has a prominent ribosome anchor located as a tip of the molecule. This tip includes the previously established unique TF signature motif. Comparison reveals that this feature is not found in SRP structures. We identify a conserved helical kink as a hallmark of the TF structure that is most likely critical to ensure ribosome association. [References: 54]
机译：核糖体的出口通道区域已被很好地确立为指导新生多肽命运的组分之间相互作用的焦点。其中之一，伴侣触发因子（TF），通过其N-末端结构域与50S核糖体亚基缔合。将TF靶向核糖体对于实现其在蛋白质折叠中的显着效率至关重要。在依赖信号识别颗粒（SRP）的蛋白质移位中发现了与翻译相似的紧密偶联。在这里，我们报告大肠杆菌TF核糖体结合域的晶体结构。 TF在结构上与Hsp33分子伴侣有关，但有一个突出的核糖体锚点位于分子的尖端。该技巧包括以前建立的独特TF签名主题。比较表明，在SRP结构中找不到此功能。我们确定保守的螺旋扭结是TF结构的标志，这对确保核糖体缔合至关重要。 [参考：54]

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