Stopped in its tracks: The RNA polymerase molecular motor as a robust sensor of DNA damage
| Autor: | Terence R. Strick, Jun Fan, K. Howan, Jordan Monnet |
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| Přispěvatelé: | Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique, University of Paris 7, EURYI award, PhD fellowship from the French Ministry of Research, Association pour la Recherche contre le Cancer, PhD fellowship from the China Science Council |
| Rok vydání: | 2014 |
| Předmět: |
DNA Repair
Transcription Genetic DNA damage DNA repair Biology medicine.disease_cause Biochemistry Helicase 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Bacterial Proteins RNA polymerase Escherichia coli medicine Molecular motor Translocase Molecular Biology 030304 developmental biology Genetics [SDV.GEN]Life Sciences [q-bio]/Genetics 0303 health sciences Endodeoxyribonucleases Escherichia coli Proteins Molecular Motor Proteins Single-molecule DNA DNA-Directed RNA Polymerases Cell Biology chemistry Magnetic trapping [SDV.TOX]Life Sciences [q-bio]/Toxicology Biophysics biology.protein Transcription Repair 030217 neurology & neurosurgery DNA Damage Protein Binding Transcription Factors |
| Zdroj: | DNA Repair (Amst) DNA Repair (Amst), 2014, epub ahead of print. ⟨10.1016/j.dnarep.2014.02.018⟩ |
| ISSN: | 1568-7864 |
| Popis: | International audience; : DNA repair is often a complex, multi-component, multi-step process; this makes detailed kinetic analysis of the different steps of repair a challenging task using standard biochemical methods. At the same time, single-molecule methods are well-suited for extracting kinetic information despite time-averaging due to diffusion of biochemical components and stochasticity of chemical reaction steps. Here we discuss recent experiments using DNA nanomanipulation in a magnetic trap to study the initiation of transcription-coupled repair in a model bacterial system comprising the canonical Escherichia coli RNA polymerase and the Mfd translocase which specifically binds to it. These experiments provide kinetic insight into the reaction process, helping to explain how Mfd discriminates between transcribing RNAP and stalled RNAP. They also identify a reliably long-lived intermediate containing Mfd translocase and, potentially, RNA polymerase. This intermediate presumably serves as a platform for assembly of downstream repair components UvrAB(C). |
| Databáze: | OpenAIRE |
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