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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Ribosomal protein S1 binds mRNA and tmRNA similarly but plays distinct roles in translation of these molecules
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Ribosomal protein S1 binds mRNA and tmRNA similarly but plays distinct roles in translation of these molecules

机译：核糖体蛋白S1类似地结合mRNA和tmRNA，但在这些分子的翻译中起不同的作用

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摘要

Ribosomes stalled during protein synthesis can be rescued by tmRNA, which-acts first as a tRNA and then as an mRNA to direct addition of a C-terminal degradation tag to the nascent polypeptide. Ribosomal protein S1 binds tmRNA, but its functional role in tmRNA-mediated tagging is uncertain. To probe interactions between S1 and tmRNA, truncated variants missing one or more of the six contiguous S1 domains were studied. The third S1 domain (R1) plays a critical role in binding tmRNA and mRNA but requires additional N- or C-terminal S1 domains. The binding of S1 and its fragments to tmRNA and mRNA is positively cooperative, and the essential role of the R1 domain may be to mediate protein-protein interactions. Overproduction of N-terminal fragments of S1 in Escherichia coli displaces endogenous S1 from ribosomes, inhibits general protein synthesis, and slows growth but causes little if any disruption of tmRNA-mediated tagging. Moreover, tagging of proteins translated from model mRNAs with either no or an increased requirement for S1 is indistinguishable. These results raise the possibility that S1 plays little or no role in tmRNA-mediated tagging.
机译：蛋白质合成过程中停滞的核糖体可以通过tmRNA抢救，tmRNA首先充当tRNA，然后充当mRNA，以将C末端降解标签直接添加到新生多肽中。核糖体蛋白S1与tmRNA结合，但是在tmRNA介导的标签中其功能性作用尚不确定。为了探测S1和tmRNA之间的相互作用，研究了缺失六个连续S1域中一个或多个的截短变体。第三个S1域（R1）在结合tmRNA和mRNA中起关键作用，但需要其他N或C端S1域。 S1及其片段与tmRNA和mRNA的结合是正向合作的，R1结构域的基本作用可能是介导蛋白质与蛋白质的相互作用。大肠杆菌中S1的N末端片段过量产生，取代了核糖体中的内源性S1，抑制了一般的蛋白质合成，并减缓了生长，但几乎不会破坏tmRNA介导的标签。而且，从模型mRNA转换而来的蛋白的标记或无标记或S1需求增加是无法区分的。这些结果提高了S1在tmRNA介导的标签中几乎没有发挥作用的可能性。

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