PMID:17110332
| Citation |
Qin, Y, Polacek, N, Vesper, O, Staub, E, Einfeldt, E, Wilson, DN and Nierhaus, KH (2006) The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome. Cell 127:721-33 |
|---|---|
| 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). |
| Links |
PubMed Online version:10.1016/j.cell.2006.09.037 |
| Keywords |
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; Phylogeny; Protein Biosynthesis/genetics; Protein Structure, Secondary; Protein Structure, Tertiary; Ribosomes/metabolism; Transcription, Genetic; Transcriptional Elongation Factors/chemistry; Transcriptional Elongation Factors/metabolism |
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