Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Elongation Factor P and the Control of Translation Elongation

Elongation Factor P and the Control of Translation Elongation 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Microbiology Annual Reviews

Elongation Factor P and the Control of Translation Elongation

Download PDF
15 pages

Loading next page...
 
/lp/annual-reviews/elongation-factor-p-and-the-control-of-translation-elongation-ZCk0KE7qqv
Publisher
Annual Reviews
Copyright
Copyright 2017 by Annual Reviews. All rights reserved
ISSN
0066-4227
eISSN
1545-3251
DOI
10.1146/annurev-micro-090816-093629
pmid
28886684
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Annual Review of Microbiology – Annual Reviews

Published: Sep 8, 2017

There are no references for this article.