PMID:10983996
| Citation |
Peske, F, Matassova, NB, Savelsbergh, A, Rodnina, MV and Wintermeyer, W (2000) Conformationally restricted elongation factor G retains GTPase activity but is inactive in translocation on the ribosome. Mol. Cell 6:501-5 |
|---|---|
| Abstract |
Elongation factor G (EF-G) from Escherichia coli is a large, five-domain GTPase that promotes tRNA translocation on the ribosome. Full activity requires GTP hydrolysis, suggesting that a conformational change of the factor is important for function. To restrict the intramolecular mobility, two cysteine residues were engineered into domains 1 and 5 of EF-G that spontaneously formed a disulfide cross-link. Cross-linked EF-G retained GTPase activity on the ribosome, whereas it was inactive in translocation as well as in turnover. Both activities were restored when the cross-link was reversed by reduction. These results strongly argue against a GTPase switch-type model of EF-G function and demonstrate that conformational mobility is an absolute requirement for EF-G function on the ribosome. |
| Links | |
| Keywords |
Amino Acid Substitution; Cross-Linking Reagents; Cysteine; Escherichia coli/metabolism; GTP Phosphohydrolases/metabolism; Guanosine Diphosphate/metabolism; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Peptide Elongation Factor G/chemistry; Peptide Elongation Factor G/metabolism; Protein Conformation; RNA, Transfer/metabolism; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Ribosomes/metabolism; Thermus thermophilus/metabolism |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.