Elongation factor Tu: a molecular switch in protein biosynthesis.
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.
Weijland
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SDI No. 61840 du CNRS, Laboratoire de Biochimie, Ecole Polytechnique, Palaiseau, France.
Harmark
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Cool
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Anborgh
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Parmeggiani
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D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D008969:Molecular Sequence Data; D010444:Peptide Elongation Factor Tu / Q000235:genetics / Q000378:metabolism*; D014176:Protein Biosynthesis / Q000502:physiology*; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D010444:Peptide Elongation Factor Tu