Rifamycins do not function by allosteric modulation of binding of Mg2+ to the RNA polymerase active center
| Autor: | Qiaorong Jiang, Herbert Irschik, Seth A. Darst, Lars F. Westblade, Rolf Jansen, Andrey Feklistov, Vladimir Mekler, Richard H. Ebright, Arkady Mustaev |
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| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Allosteric regulation
genetic processes Rifamycins Active center chemistry.chemical_compound Allosteric Regulation RNA polymerase polycyclic compounds Magnesium Polymerase Multidisciplinary Binding Sites biology Rifamycin RNA DNA-Directed RNA Polymerases Biological Sciences Anti-Bacterial Agents A-site enzymes and coenzymes (carbohydrates) chemistry Biochemistry Mutation biology.protein Biophysics health occupations bacteria |
| Popis: | Rifamycin antibacterial agents inhibit bacterial RNA polymerase (RNAP) by binding to a site adjacent to the RNAP active center and preventing synthesis of RNA products >2–3 nt in length. Recently, Artsimovitch et al. [(2005) Cell 122:351–363] proposed that rifamycins function by allosteric modulation of binding of Mg 2+ to the RNAP active center and presented three lines of biochemical evidence consistent with this proposal. Here, we show that rifamycins do not affect the affinity of binding of Mg 2+ to the RNAP active center, and we reassess the three lines of biochemical evidence, obtaining results not supportive of the proposal. We conclude that rifamycins do not function by allosteric modulation of binding of Mg 2+ to the RNAP active center. |
| Databáze: | OpenAIRE |
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