ArticleNature2016
Reconstruction of bacterial transcription-coupled repair at single-molecule resolution.
Article in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
51 citing papers in PubMed, 88 citations in OpenAlex.
- Structural basis for loading of transcription repair-coupling factor Mfd onto stalled elongation complexes.Nucleic acids research · 2026Article
- The ω subunit stabilizes transcribing RNA polymerase to balance processivity and collision resolution.bioRxiv : the preprint server for biology · 2026Article
- Genome-wide strand-specific UV mutagenesis inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis for loading of Transcription Repair-Coupling factor Mfd onto stalled elongation complexes.bioRxiv : the preprint server for biology · 2025Article
- Participants in Transcription-Replication Conflict and Their Role in Formation and Resolution of R-Loops.International journal of molecular sciences · 2025Review
- Dynamics of transcription-coupled repair of cyclobutane pyrimidine dimers and (6-4) photoproducts inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Insight into Single-Molecule Imaging Techniques for the Study of Prokaryotic Genome Maintenance.Chemical & biomedical imaging · 2024Review
- 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
- Regulation of bacterial gene expression by non-coding RNA: It is all about time!Cell chemical biology · 2024Review
- Shifted PAMs generate DNA overhangs and enhance SpCas9 post-catalytic complex dissociation.Nature structural & molecular biology · 2023Article
- Article
- On the stability of stalled RNA polymerase and its removal by RapA.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
- 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli Mfd translocase enables transcription-coupled repair by displacing RNA polymerase (RNAP) stalled on a DNA lesion and then coordinating assembly of the UvrAB(C) components at the damage site. Recent studies have shown that after binding to and dislodging stalled RNAP, Mfd remains on the DNA in the form of a stable, slowly translocating complex with evicted RNAP attached. Here we find, using a series of single-molecule assays, that recruitment of UvrA and UvrAB to Mfd-RNAP arrests the translocating complex and causes its dissolution. Correlative single-molecule nanomanipulation and fluorescence measurements show that dissolution of the complex leads to loss of both RNAP and Mfd. Subsequent DNA incision by UvrC is faster than when only UvrAB(C) are available, in part because UvrAB binds 20-200 times more strongly to Mfd–RNAP than to DNA damage. These observations provide a quantitative framework for comparing complementary DNA repair pathways in vivo.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.