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延伸因子EF-P与大肠杆菌核糖体的相互作用。

Interactions of elongation factor EF-P with the Escherichia coli ribosome.

作者信息

Aoki Hiroyuki, Xu John, Emili Andrew, Chosay John G, Golshani Ashkan, Ganoza M Clelia

机构信息

University of Toronto, C.H. Best Institute, Canada.

出版信息

FEBS J. 2008 Feb;275(4):671-81. doi: 10.1111/j.1742-4658.2007.06228.x. Epub 2008 Jan 12.

Abstract

EF-P (eubacterial elongation factor P) is a highly conserved protein essential for protein synthesis. We report that EF-P protects 16S rRNA near the G526 streptomycin and the S12 and mRNA binding sites (30S T-site). EF-P also protects domain V of the 23S rRNA proximal to the A-site (50S T-site) and more strongly the A-site of 70S ribosomes. We suggest that EF-P: (a) may play a role in translational fidelity and (b) prevents entry of fMet-tRNA into the A-site enabling it to bind to the 50S P-site. We also report that EF-P promotes a ribosome-dependent accommodation of fMet-tRNA into the 70S P-site.

摘要

真细菌延伸因子P(EF-P)是一种对蛋白质合成至关重要的高度保守蛋白。我们报告称,EF-P可保护靠近G526链霉素以及S12和mRNA结合位点(30S T位点)的16S rRNA。EF-P还可保护靠近A位点(50S T位点)的23S rRNA的结构域V,并且对70S核糖体的A位点保护作用更强。我们认为EF-P:(a)可能在翻译保真度中发挥作用,(b)阻止甲酰甲硫氨酰-tRNA进入A位点,使其能够结合到50S P位点。我们还报告称,EF-P可促进核糖体依赖性地将甲酰甲硫氨酰-tRNA容纳到70S P位点。

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