| Literature DB >> 17110332 |
Yan Qin1, Norbert Polacek, Oliver Vesper, Eike Staub, Edda Einfeldt, Daniel N Wilson, Knud H Nierhaus.
Abstract
The ribosomal elongation cycle describes a series of reactions prolonging the nascent polypeptide chain by one amino acid and driven by two universal elongation factors termed EF-Tu and EF-G in bacteria. Here we demonstrate that the extremely conserved LepA protein, present in all bacteria and mitochondria, is a third elongation factor required for accurate and efficient protein synthesis. LepA has the unique function of back-translocating posttranslocational ribosomes, and the results suggest that it recognizes ribosomes after a defective translocation reaction and induces a back-translocation, thus giving EF-G a second chance to translocate the tRNAs correctly. We suggest renaming LepA as elongation factor 4 (EF4).Entities:
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Year: 2006 PMID： 17110332 DOI： 10.1016/j.cell.2006.09.037
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582