Elongation factor Tu: a molecular switch in protein biosynthesis
- 1 March 1992
- journal article
- review article
- Published by Wiley in Molecular Microbiology
- Vol. 6 (6) , 683-688
- https://doi.org/10.1111/j.1365-2958.1992.tb01516.x
Abstract
Summary: 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 Å 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.Keywords
This publication has 60 references indexed in Scilit:
- Refined structure of elongation factor EF-Tu from Escherichia coliJournal of Molecular Biology, 1992
- Crystals of intact elongation factor Tu from Thermus thermophilus diffracting to high resolutionJournal of Molecular Biology, 1991
- The GTPase superfamily: conserved structure and molecular mechanismNature, 1991
- Both genes for EF-Tu in Salmonella typhimurium are individually dispensable for growthJournal of Molecular Biology, 1990
- Antisuppression by mutations in elongation factor TuEuropean Journal of Biochemistry, 1990
- How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?Journal of Molecular Biology, 1990
- Homologies in the Structures of G-Binding Proteins: An Analysis Based on Elongation Factor EF-TUNature Biotechnology, 1989
- Crosslinking of elongation factor Tu to tRNAPhe by trans‐diamminedichloroplatinum (II) Characterization of two crosslinking sites on EF‐TuFEBS Letters, 1989
- Structural features in aminoacyl‐tRNAs required for recognition by elongation factor TuFEBS Letters, 1987