Literature DB >> 1573997

Elongation factor Tu: a molecular switch in protein biosynthesis.

A Weijland1, K Harmark, R H Cool, P H Anborgh, A Parmeggiani.   

Abstract

Elongation factor Tu (EF-Tu), the most abundant protein in Escherichia coli, is a guanine nucleotide-binding protein that in the 'on' state acts as a carrier of amino acyl-tRNA to the ribosome. Our knowledge of this essential component of translation has brought substantial progress in the past decade thanks to the co-ordinated application of biochemical, physico-chemical and genetic methods. Crystallographic analysis at 2.6 A resolution and site-directed mutagenesis have revealed structural and functional similarities between the guanine nucleotide-binding domains of EF-Tu and human H-ras p21 protein. The regulation of the expression of the two EF-Tu-encoding genes in E. coli, particularly that of tufB, has been shown to involve diverse mechanisms. Several aspects of the functions of EF-Tu in the elongation cycle have been reinvestigated, leading to new insights. These studies have emphasized the manifold aspects of the mechanisms regulating the activity of EF-Tu in the bacterial cell.

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Year:  1992        PMID: 1573997     DOI: 10.1111/j.1365-2958.1992.tb01516.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  21 in total

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2.  The amino acid valine is secreted in continuous-flow bacterial biofilms.

Authors:  Jaione Valle; Sandra Da Re; Solveig Schmid; David Skurnik; Richard D'Ari; Jean-Marc Ghigo
Journal:  J Bacteriol       Date:  2007-11-02       Impact factor: 3.490

3.  Proteomic studies of an Antarctic cold-adapted bacterium, Shewanella livingstonensis Ac10, for global identification of cold-inducible proteins.

Authors:  Jun Kawamoto; Tatsuo Kurihara; Masanari Kitagawa; Ikunoshin Kato; Nobuyoshi Esaki
Journal:  Extremophiles       Date:  2007-07-07       Impact factor: 2.395

4.  Direct detection of viable bacteria, molds, and yeasts by reverse transcriptase PCR in contaminated milk samples after heat treatment.

Authors:  M Vaitilingom; F Gendre; P Brignon
Journal:  Appl Environ Microbiol       Date:  1998-03       Impact factor: 4.792

5.  Doc toxin is a kinase that inactivates elongation factor Tu.

Authors:  Jonathan W Cruz; Francesca P Rothenbacher; Tatsuya Maehigashi; William S Lane; Christine M Dunham; Nancy A Woychik
Journal:  J Biol Chem       Date:  2014-01-21       Impact factor: 5.157

6.  In vivo selection of conditional-lethal mutations in the gene encoding elongation factor G of Escherichia coli.

Authors:  Y Hou; Y P Lin; J D Sharer; P E March
Journal:  J Bacteriol       Date:  1994-01       Impact factor: 3.490

Review 7.  Peptide-chain elongation in eukaryotes.

Authors:  C G Proud
Journal:  Mol Biol Rep       Date:  1994-05       Impact factor: 2.316

8.  Carboxyl-terminal amino acid residues in elongation factor G essential for ribosome association and translocation.

Authors:  Y Hou; E S Yaskowiak; P E March
Journal:  J Bacteriol       Date:  1994-11       Impact factor: 3.490

9.  Inactivation of the elongation factor Tu by mosquitocidal toxin-catalyzed mono-ADP-ribosylation.

Authors:  Jörg Schirmer; Hans-Joachim Wieden; Marina V Rodnina; Klaus Aktories
Journal:  Appl Environ Microbiol       Date:  2002-10       Impact factor: 4.792

10.  A technique for targeted mutagenesis of the EF-Tu chromosomal gene by M13-mediated gene replacement.

Authors:  L A Zeef; L Bosch
Journal:  Mol Gen Genet       Date:  1993-04
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