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Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome
Open accessAbstract
The region around position 1067 in domain II of 23S rRNA frequently is referred to as the GTPase center of the ribosome. The notion is based on the observation that the binding of the antibiotic thiostrepton to this region inhibited GTP hydrolysis by elongation factor G (EF-G) on the ribosome at the conditions of multiple turnover. In the present work, we have reanalyzed the mechanism of action of thiostrepton. Results obtained by biochemical and fast kinetic techniques show that thiostrepton binding to the ribosome does not interfere with factor binding or with single-round GTP hydrolysis. Rather, the antibiotic inhibits the function of EF-G in subsequent steps, including release of inorganic phosphate from EF-G after GTP hydrolysis, tRNA translocation, and the dissociation of the factor from the ribosome, thereby inhibiting the turnover reaction. Structurally, thiostrepton interferes with EF-G footprints in the α-sarcin stem loop (A2660, A2662) located in domain VI of 23S rRNA. The results indicate that thiostrepton inhibits a structural transition of the 1067 region of 23S rRNA that is important for functions of EF-G after GTP hydrolysis.
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Cited by
Arnison, P. G., Bibb, M. J., Bierbaum, G., Bowers, A. A., Bugni, T. S., Bulaj, G., Camarero, J. A., Campopiano, D. J., Challis, G. L., Clardy, J., et al. (2013) · Nat. Prod. Rep. · doi:10.1039/c2np20085f · Cited by 2,076
Ribosome Structure and the Mechanism of Translation
Ramakrishnan, V. (2002) · Cell · doi:10.1016/s0092-8674(02)00619-0 · Cited by 938
The bacterial ribosome as a target for antibiotics
Poehlsgaard, J., & Douthwaite, S. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1265 · Cited by 607
The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State
Gao, Y.-G., Selmer, M., Dunham, C. M., Weixlbaumer, A., Kelley, A. C., & Ramakrishnan, V. (2009) · Science · doi:10.1126/science.1179709 · Cited by 513
Structure of the E. coli ribosome–EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM
Fischer, N., Neumann, P., Konevega, A. L., Bock, L. V., Ficner, R., Rodnina, M. V., & Stark, H. (2015) · Nature · doi:10.1038/nature14275 · Cited by 362
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Metadata
- Authors
- Rodnina, M. V., Savelsbergh, A., Matassova, N. B., Katunin, V. I., Semenkov, Y. P., & Wintermeyer, W.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1999-08-17
- Volume
- 96
- Issue
- 17
- Pages
- 9586-9590
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2069885328
- Cited by
- 186
- References
- 0
- FWCI
- 2.61
- Type
- journal article
- Language
- en
- Open access
- green
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- Rodnina, M. V., Savelsbergh, A., Matassova, N. B., Katunin, V. I., Semenkov, Y. P., & Wintermeyer, W. (1999). Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.17.9586
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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