The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosorne

被引：167

作者：

Qin, Yan

Polacek, Norbert

Vesper, Oliver

Staub, Eike

Einfeldt, Edda

Wilson, Daniel N.

Nierhaus, Knud H.

机构：

[1] Max Planck Inst Mol Genet, D-14195 Berlin, Germany

[2] Innsbruck Med Univ, Div Genom & RNomics, Bioctr, A-6020 Innsbruck, Austria

来源：

CELL | 2006年 / 127卷 / 04期

基金：

奥地利科学基金会;

关键词：

TRANSFER-RNA; ESCHERICHIA-COLI; SIGNAL PEPTIDASE; FACTOR-TU; P-SITES; A-SITES; BINDING; PROTEIN; GENE; SUBUNIT;

D O I：

10.1016/j.cell.2006.09.037

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The ribosomal elongation cycle describes a series of reactions prolonging the nascent poly-pepticle 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 post-translocational 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).

引用

收藏

页码：721 / 733

页数：13

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