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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Savelsbergh, Andreas Rodnina, Marina V. Wilden, Berthold Wintermeyer, Wolfgang |
| Description | Author Affiliation: Wilden B ( Institutes of Molecular Biology and Physical Biochemistry, University of Witten-Herdecke, D-58448 Witten, Germany.); |
| Abstract | The translocation of tRNA and mRNA through the ribosome is promoted by elongation factor G (EF-G), a GTPase that hydrolyzes GTP during the reaction. Recently, it was reported that, in contrast to previous observations, the affinity of EF-G was much weaker for GTP than for GDP and that ribosome-catalyzed GDP-GTP exchange would be required for translocation [Zavialov AV, Hauryliuk VV, Ehrenberg M (2005) J Biol 4:9]. We have reinvestigated GTP/GDP binding and show that EF-G binds GTP and GDP with affinities in the 20 to 40 microM range (37 degrees C), in accordance with earlier reports. Furthermore, GDP exchange, which is extremely rapid on unbound EF-G, is retarded, rather than accelerated, on the ribosome, which, therefore, is not a nucleotide-exchange factor for EF-G. The EF-G.GDPNP complex, which is very labile, is stabilized 30,000-fold by binding to the ribosome. These findings, together with earlier kinetic results, reveal that EF-G enters the pretranslocation ribosome in the GTP-bound form and indicate that, upon ribosome-complex formation, the nucleotide-binding pocket of EF-G is closed, presumably in conjunction with GTPase activation. GTP hydrolysis is required for rapid tRNA-mRNA movement, and P(i) release induces further rearrangements of both EF-G and the ribosome that are required for EF-G turnover. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 37 |
| Volume Number | 103 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2006-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Guanosine Triphosphate Chemistry Peptide Elongation Factor G RNA, Transfer Ribosomes Dissociative Disorders Escherichia Coli Enzymology Metabolism Hydrolysis Kinetics Thermotoga Maritima Thermus Thermophilus Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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