ArticleNucleic acids research2010
Structural basis for the bacterial transcription-repair coupling factor/RNA polymerase interaction.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 70 citations in OpenAlex.
- Multiple classes and isoforms of the RNA polymerase recycling motor protein HelD.MicrobiologyOpen · 2021Article
- Article
- 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 majority ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural basis of Mfd-dependent transcription termination.Nucleic acids research · 2020Article
- UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain.Communications biology · 2020Article
- Structure-Guided Designing and Evaluation of Peptides Targeting Bacterial Transcription.Frontiers in bioengineering and biotechnology · 2020Article
- CarD and RbpA modify the kinetics of initial transcription and slow promoter escape of the Mycobacterium tuberculosis RNA polymerase.Nucleic acids research · 2019Article
- The transcription-repair coupling factor Mfd associates with RNA polymerase in the absence of exogenous damage.Nature communications · 2018Article
- Helicases as transcription termination factors: Different solutions for a common problem.Transcription · 2018Article
- Structural basis of arrestin-3 activation and signaling.Nature communications · 2017Article
- Mechanistic insights into transcription coupled DNA repair.DNA repair · 2017Review
- The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase.Nucleic acids research · 2017Article
- Mfd Protein and Transcription-Repair Coupling in Escherichia coli.Photochemistry and photobiology · 2017Review
- Reconstruction of bacterial transcription-coupled repair at single-molecule resolution.Nature · 2016Article
- ppGpp couples transcription to DNA repair in E. coli.Science (New York, N.Y.) · 2016Article
- CarD uses a minor groove wedge mechanism to stabilize the RNA polymerase open promoter complex.eLife · 2015Article
- A dynamic DNA-repair complex observed by correlative single-molecule nanomanipulation and fluorescence.Nature structural & molecular biology · 2015Article
- Structural biology of bacterial RNA polymerase.Biomolecules · 2015Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The transcription-repair coupling factor (TRCF, the product of the mfd gene) is a widely conserved bacterial protein that mediates transcription-coupled DNA repair. TRCF uses its ATP-dependent DNA translocase activity to remove transcription complexes stalled at sites of DNA damage, and stimulates repair by recruiting components of the nucleotide excision repair pathway to the site. A protein/protein interaction between TRCF and the β-subunit of RNA polymerase (RNAP) is essential for TRCF function. CarD (also called CdnL), an essential regulator of rRNA transcription in Mycobacterium tuberculosis, shares a homologous RNAP interacting domain with TRCF and also interacts with the RNAP β-subunit. We determined the 2.9-Å resolution X-ray crystal structure of the RNAP interacting domain of TRCF complexed with the RNAP-β1 domain, which harbors the TRCF interaction determinants. The structure reveals details of the TRCF/RNAP protein/protein interface, providing a basis for the design and interpretation of experiments probing TRCF, and by homology CarD, function and interactions with the RNAP.
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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.