Elongation factor Tu: a molecular switch in protein biosynthesis |
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Authors: | Albert Weijland,Kim Harmark,Robbert H. Cool,&dagger ,Pieter H. Anborgh,rea Parmeggiani |
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Affiliation: | SDI No. 61840 du CNRS, Laboratoire de Biochimie, Ecole Polytechnique, Palaiseau, France. |
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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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