ArticleNature structural & molecular biology2015
A dynamic DNA-repair complex observed by correlative single-molecule nanomanipulation and fluorescence.
Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Structural basis for loading of transcription repair-coupling factor Mfd onto stalled elongation complexes.Nucleic acids research · 2026Article
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Structural basis for loading of Transcription Repair-Coupling factor Mfd onto stalled elongation complexes.bioRxiv : the preprint server for biology · 2025Article
- Single-molecule reconstruction of eukaryotic factor-dependent transcription termination.Nature communications · 2024Article
- Single-molecule characterization of Sen1 translocation properties provides insights into eukaryotic factor-dependent transcription termination.Nucleic acids research · 2024Article
- Shifted PAMs generate DNA overhangs and enhance SpCas9 post-catalytic complex dissociation.Nature structural & molecular biology · 2023Article
- On the stability of stalled RNA polymerase and its removal by RapA.Nucleic acids research · 2022Article
- Efficient golden gate assembly of DNA constructs for single molecule force spectroscopy and imaging.Nucleic acids research · 2022Article
- Mechanism of transcription modulation by the transcription-repair coupling factor.Nucleic acids research · 2022Article
- Single-molecule studies of helicases and translocases in prokaryotic genome-maintenance pathways.DNA repair · 2021Review
- Mfd - at the crossroads of bacterial DNA repair, transcriptional regulation and molecular evolvability.Transcription · 2021Review
- Cotranscriptional R-loop formation by Mfd involves topological partitioning of DNA.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Parallel, linear, and subnanometric 3D tracking of microparticles with Stereo Darkfield Interferometry.Science advances · 2021Article
- Detection of genetic variation and base modifications at base-pair resolution on both DNA and RNA.Communications biology · 2021Article
- Article
- A Peek Inside the Machines of Bacterial Nucleotide Excision Repair.International journal of molecular sciences · 2021Review
- The Transcription-Repair Coupling Factor Mfd Prevents and Promotes Mutagenesis in a Context-Dependent Manner.Frontiers in molecular biosciences · 2021Review
- Molecular determinants for dsDNA translocation by the transcription-repair coupling and evolvability factor Mfd.Nature communications · 2020Article
- Direct observation of helicase-topoisomerase coupling within reverse gyrase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Single-molecule live-cell imaging visualizes parallel pathways of prokaryotic nucleotide excision repair.Nature communications · 2020Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We characterize in real time the composition and catalytic state of the initial Escherichia coli transcription-coupled repair (TCR) machinery by using correlative single-molecule methods. TCR initiates when RNA polymerase (RNAP) stalled by a lesion is displaced by the Mfd DNA translocase, thus giving repair components access to the damage. We previously used DNA nanomanipulation to obtain a nanomechanical readout of protein-DNA interactions during TCR initiation. Here we correlate this signal with simultaneous single-molecule fluorescence imaging of labeled components (RNAP, Mfd or RNA) to monitor the composition and localization of the complex. Displacement of stalled RNAP by Mfd results in loss of nascent RNA but not of RNAP, which remains associated with Mfd as a long-lived complex on the DNA. This complex translocates at ∼4 bp/s along the DNA, in a manner determined by the orientation of the stalled RNAP on the DNA.
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