RNA polymerase motions during promoter melting
| Autor: | Jesse Hauver, Robert Landick, Andrey Feklistov, Karl-Heinz Altmann, Brian Bae, Agnieszka Lass-Napiorkowska, Tomasz Heyduk, Markus Kalesse, Seth A. Darst, Florian Glaus |
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| Přispěvatelé: | Helmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany. |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Models Molecular Rotation Movement genetic processes Static Electricity Biology Ligands Nucleic Acid Denaturation Article 03 medical and health sciences Nucleic acid thermodynamics chemistry.chemical_compound 0302 clinical medicine Genes Reporter RNA polymerase Catalytic Domain Promoter Regions Genetic Gene Polymerase Multidisciplinary DNA clamp Bacteria RNA Promoter DNA DNA-Directed RNA Polymerases Templates Genetic enzymes and coenzymes (carbohydrates) Kinetics 030104 developmental biology Biochemistry chemistry biology.protein Biophysics health occupations bacteria Nucleic Acid Conformation Crystallization 030217 neurology & neurosurgery |
| Popis: | Trapping RNA polymerase in the act The enzyme RNA polymerase (RNAP) finds promoter elements in the genome, separates (or “melts”) the DNA strands, and transcribes the template DNA strand to give RNA. A mobile clamp in RNAP plays a key role in initiating transcription. Feklistov et al. locked the clamp of bacterial RNAP in distinct conformations by using small molecules. They then used fluorescent probes to monitor binding as the promoter DNA was separated. Unexpectedly, they found that the clamp transiently closed to nucleate DNA melting, opened to load single-stranded DNA into the active site, and then closed around the template strand to start transcription. Science , this issue p. 863 |
| Databáze: | OpenAIRE |
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