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Elongation Factor P and the Control of Translation Elongation
Annual Review of Microbiology ( IF 8.5 ) Pub Date : 2017-09-08 00:00:00 , DOI: 10.1146/annurev-micro-090816-093629
Andrei Rajkovic 1 , Michael Ibba 1, 2
Affiliation  

Elongation factor P (EF-P) binds to ribosomes requiring assistance with the formation of oligo-prolines. In order for EF-P to associate with paused ribosomes, certain tRNAs with specific d-arm residues must be present in the peptidyl site, e.g., tRNAPro. Once EF-P is accommodated into the ribosome and bound to Pro-tRNAPro, productive synthesis of the peptide bond occurs. The underlying mechanism by which EF-P facilitates this reaction seems to have entropic origins. Maximal activity of EF-P requires a posttranslational modification in Escherichia coli, Pseudomonas aeruginosa, and Bacillus subtilis. Each of these modifications is distinct and ligated onto its respective EF-P through entirely convergent means. Here we review the facets of translation elongation that are controlled by EF-P, with a particular focus on the purpose behind the many different modifications of EF-P.

中文翻译:


延伸因子P与翻译延伸的控制

延伸因子P(EF-P)与需要辅助寡脯氨酸形成的核糖体结合。为了使EF-P与悬浮的核糖体缔合,某些带有特定d臂残基的tRNA必须存在于肽基位点,例如tRNA Pro。一旦将EF-P容纳到核糖体中并与Pro-tRNA Pro结合,就会发生肽键的高效合成。EF-P促进该反应的潜在机制似乎来自熵。EF-P的最大活性需要在大肠杆菌铜绿假单胞菌枯草芽孢杆菌中进行翻译后修饰。这些修饰中的每一个都是不同的,并通过完全收敛的方式连接到其各自的EF-P上。在这里,我们回顾了由EF-P控制的翻译延伸方面,尤其着重于EF-P的许多不同修改背后的目的。

更新日期:2017-09-08
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