Abstract
Fluoroaluminates are thought to mimic the γ‐phosphate of GTP and thus, together with GDP, perturb the functioning of heterotrimeric GTP‐binding G‐proteins. Here we show they do inhibit the ribosome‐stimulated GTPase activity of EF‐G from Escherichia coli via the formation of a stable complex with EF‐G·GDP and ribosomes. In contrast, no perturbed interactions were observed in a similar ribosomal complex with EF‐Tu. Interestingly, in the absence of ribosomes both EF‐Tu and EF‐G remain totally unaffected by fluoroaluminates. For members of the GTPase superfamily such differential effects have not been described before.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 5:09 a.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 3:17 p.m.) |
Indexed | 1 year, 7 months ago (Jan. 13, 2024, 12:28 a.m.) |
Issued | 32 years, 4 months ago (April 26, 1993) |
Published | 32 years, 4 months ago (April 26, 1993) |
Published Online | 23 years, 10 months ago (Nov. 1, 2001) |
Published Print | 32 years, 4 months ago (April 26, 1993) |
@article{Mesters_1993, title={Divergent effects of fluoroaluminates on the peptide chain elongation factors EF‐Tu and EF‐G as members of the GTPase superfamily}, volume={321}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(93)80097-e}, DOI={10.1016/0014-5793(93)80097-e}, number={2–3}, journal={FEBS Letters}, publisher={Wiley}, author={Mesters, Jeroen R. and de Graaf, J.Martien and Kraal, Barend}, year={1993}, month=apr, pages={149–152} }