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

Pech, M., Karim, Z., Yamamoto, H., Kitakawa, M., Qin, Y., & Nierhaus, K. H. (2011). Elongation factor 4 (EF4/LepA) accelerates protein synthesis at increased Mg2+ concentrations. Proc Natl Acad Sci U S A, 108(8), 3199-203. Retrieved from http://www.pnas.org/content/108/8/3199.full.pdf.

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 Creators:
Pech, M.1, Author              
Karim, Z., Author
Yamamoto, H.2, Author              
Kitakawa, M., Author
Qin, Y.3, Author              
Nierhaus, K. H.3, Author              
Affiliations:
1Dept. of Computational Molecular Biology (Head: Martin Vingron), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433547              
2Dept. of Human Molecular Genetics (Head: Hans-Hilger Ropers), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433549              
3Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              

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Free keywords: Escherichia coli/growth & development; Escherichia coli Proteins/ metabolism/physiology; Magnesium/pharmacology; Osmolar Concentration; Protein Biosynthesis/ genetics; Protein Transport; Ribosomes/pathology; Temperature; Transcriptional Elongation Factors/ metabolism/physiology
 Abstract: 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(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 or low temperatures explains the ubiquitous distribution and high conservation of EF4.

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 Dates: 2011
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: eDoc: 584591
URI: http://www.pnas.org/content/108/8/3199.full.pdf
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Title: Proc Natl Acad Sci U S A
Source Genre: Journal
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Pages: - Volume / Issue: 108 (8) Sequence Number: - Start / End Page: 3199 - 203 Identifier: ISSN: 1091-6490 (Electronic) 0027-8424 (Linking)