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

Cell. 2006 Nov 17;127(4):721-33. doi: 10.1016/j.cell.2006.09.037.

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).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Computational Biology
  • Conserved Sequence*
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / metabolism*
  • GTP Phosphohydrolases / metabolism
  • Green Fluorescent Proteins / metabolism
  • Models, Genetic
  • Molecular Sequence Data
  • Peptide Elongation Factor G / chemistry
  • Peptide Elongation Factors / metabolism*
  • Peptide Initiation Factors
  • Phylogeny
  • Protein Biosynthesis / genetics*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Ribosomes / metabolism*
  • Transcription, Genetic
  • Transcriptional Elongation Factors / chemistry
  • Transcriptional Elongation Factors / metabolism*

Substances

  • Escherichia coli Proteins
  • LepA protein, E coli
  • Peptide Elongation Factor G
  • Peptide Elongation Factors
  • Peptide Initiation Factors
  • Transcriptional Elongation Factors
  • Green Fluorescent Proteins
  • GTP Phosphohydrolases