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Elongation factor 4 (EF4/LepA) accelerates protein synthesis at increased Mg2+ concentrations

Proceedings Of The National Academy Of Sciences Of The United States Of Ame, 2011 Feb 22, Vol.108(8), pp.3199-3203 [Peer Reviewed Journal]

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  • Title:
    Elongation factor 4 (EF4/LepA) accelerates protein synthesis at increased Mg2+ concentrations
  • Author: Pech, M ; Karim, Z ; Yamamoto, H ; Kitakawa, M ; Qin, Y ; Nierhaus, Kh
  • Found In: Proceedings Of The National Academy Of Sciences Of The United States Of Ame, 2011 Feb 22, Vol.108(8), pp.3199-3203 [Peer Reviewed Journal]
  • Subjects: Mitochondrial Dna -- Physiological Aspects ; Mitochondrial Dna -- Research ; Protein Synthesis -- Physiological Aspects ; Protein Synthesis -- Research ; Proteins -- Physiological Aspects ; Proteins -- Research
  • Language: English
  • Description: Elongation factor 4 (EF4) is one of the most conserved proteins present in bacteria as well as in mitochondria and chloroplasts of eukaryotes. Although EF4 has the unique ability to catalyze the back-translocation reaction on posttranslocation state ribosomes, the physiological role of EF4 remains unclear. Here we demonstrate that EF4 is stored at the membrane of Escherichia coli cells and released into the cytoplasm upon conditions of high ionic strength or low temperature. Under such conditions, wild-type E. coli cells overgrow mutant cells lacking the EF4 gene within 5-10 generations. Elevated intracellular [Mg.sup.2+] concentrations or low temperature retard bacterial growth and inhibit protein synthesis, probably because of formation of aberrant elongating ribosomal states. We suggest that EF4 binds to these stuck ribosomes and remobilizes them, consistent with the EF4-dependent enhancement (fivefold) in protein synthesis observed under these unfavorable conditions. The strong selective advantage conferred by the presence of EF4 at high intracellular ionic strength of low temperatures explains the ubiquitous distribution and high conservation of EF4. bacterial membrane | protein synthesis under stress doi/ 10.1073/pnas.1012994108
  • Identifier: ISSN: 0027-8424 ; DOI: 10.1073/pnas.1012994108

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