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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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資料種別: 学術論文

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 作成者:
Pech, M.1, 著者           
Karim, Z., 著者
Yamamoto, H.2, 著者           
Kitakawa, M., 著者
Qin, Y.3, 著者           
Nierhaus, K. H.3, 著者           
所属:
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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キーワード: 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
 要旨: 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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 日付: 2011
 出版の状態: 出版
 ページ: -
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 識別子(DOI, ISBNなど): eDoc: 584591
URI: http://www.pnas.org/content/108/8/3199.full.pdf
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出版物名: Proc Natl Acad Sci U S A
種別: 学術雑誌
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出版社, 出版地: -
ページ: - 巻号: 108 (8) 通巻号: - 開始・終了ページ: 3199 - 203 識別子(ISBN, ISSN, DOIなど): ISSN: 1091-6490 (Electronic) 0027-8424 (Linking)