ArticleProceedings of the National Academy of Sciences of the United States of America2012
Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
33 citing papers in PubMed, 43 citations in OpenAlex.
- Structural basis for loading of transcription repair-coupling factor Mfd onto stalled elongation complexes.Nucleic acids research · 2026Article
- Structural basis for loading of Transcription Repair-Coupling factor Mfd onto stalled elongation complexes.bioRxiv : the preprint server for biology · 2025Article
- A small molecule that inhibits the evolution of antibiotic resistance.NAR molecular medicine · 2024Article
- Mechanism of transcription modulation by the transcription-repair coupling factor.Nucleic acids research · 2022Article
- Article
- 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
- 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
- Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase ρ.Science (New York, N.Y.) · 2021Article
- Structural basis of Mfd-dependent transcription termination.Nucleic acids research · 2020Article
- Archaeal DNA Repair Mechanisms.Biomolecules · 2020Review
- Molecular determinants for dsDNA translocation by the transcription-repair coupling and evolvability factor Mfd.Nature communications · 2020Article
- Single-molecule imaging reveals molecular coupling between transcription and DNA repair machinery in live cells.Nature communications · 2020Article
- Single-molecule live-cell imaging visualizes parallel pathways of prokaryotic nucleotide excision repair.Nature communications · 2020Article
- The transcription-repair coupling factor Mfd associates with RNA polymerase in the absence of exogenous damage.Nature communications · 2018Article
- UvrA expression ofJournal of food science and technology · 2017Article
- Mfd Protein and Transcription-Repair Coupling in Escherichia coli.Photochemistry and photobiology · 2017Review
- From Mfd to TRCF and Back Again-A Perspective on Bacterial Transcription-coupled Nucleotide Excision Repair.Photochemistry and photobiology · 2017Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Transcription-coupled DNA repair targets DNA lesions that block progression of elongating RNA polymerases. In bacteria, the transcription-repair coupling factor (TRCF; also known as Mfd) SF2 ATPase recognizes RNA polymerase stalled at a site of DNA damage, removes the enzyme from the DNA, and recruits the Uvr(A)BC nucleotide excision repair machinery via UvrA binding. Previous studies of TRCF revealed a molecular architecture incompatible with UvrA binding, leaving its recruitment mechanism unclear. Here, we examine the UvrA recognition determinants of TRCF using X-ray crystallography of a core TRCF-UvrA complex and probe the conformational flexibility of TRCF in the absence and presence of nucleotides using small-angle X-ray scattering. We demonstrate that the C-terminal domain of TRCF is inhibitory for UvrA binding, but not RNA polymerase release, and show that nucleotide binding induces concerted multidomain motions. Our studies suggest that autoinhibition of UvrA binding in TRCF may be relieved only upon engaging the DNA damage.
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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.