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