一种新型细菌翻译因子 RF3 突变提示了特定的结构域用于过早的肽酰-tRNA 脱落。

A novel class of bacterial translation factor RF3 mutations suggests specific structural domains for premature peptidyl-tRNA drop-off.

机构信息

Department of Basic Medical Sciences, Institute of Medical Science, University of Tokyo (IMSUT), Tokyo, Japan.

出版信息

FEBS Lett. 2010 Feb 19;584(4):790-4. doi: 10.1016/j.febslet.2009.12.048. Epub 2009 Dec 30.

DOI:10.1016/j.febslet.2009.12.048

PMID:20043913

Abstract

The bacterial translation factor RF3 promotes translation termination by recycling the tRNA-mimicking release factors, RF1 and RF2, after mature polypeptide release. RF3 also enhances the premature peptidyl-tRNA drop-off reaction in the presence of RRF and EF-G. Despite the recently resolved X-ray crystal structure of RF3, the molecular details of the bimodal functionality of RF3 remain obscure. In this report, we demonstrate a novel class of RF3 mutations specifically defective in the tRNA drop-off reaction. These mutations suggest differential molecular pathways closely related to the guanine nucleotide modes of RF3.

摘要

细菌翻译因子 RF3 通过在成熟多肽释放后回收 tRNA 模拟释放因子 RF1 和 RF2，促进翻译终止。RF3 还增强了在 RRF 和 EF-G 存在下的过早肽酰-tRNA 脱落反应。尽管最近解析了 RF3 的 X 射线晶体结构，但 RF3 的双模态功能的分子细节仍然不清楚。在本报告中，我们证明了一类新的 RF3 突变体，它们在 tRNA 脱落反应中特异性缺陷。这些突变提示了与 RF3 的鸟嘌呤核苷酸模式密切相关的不同分子途径。