ArticleNucleic acids research2017
The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 38 citations in OpenAlex.
- Genetic analysis of epistasis between nucleotide excision repair and homologous recombination in the recovery of persisters after fluoroquinolone treatment.PLoS genetics · 2026Article
- In vivo nucleotide excision repair by mycobacterial UvrD1 requires ATP hydrolysis but does not depend on cysteine disulfide-mediated dimerization and DNA unwinding.Nucleic acids research · 2025Article
- Structural basis for dimerization and activation of UvrD-family helicases.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Hallmarks of DNA replication stress responses in Escherichia coli and Bacillus subtilis.FEMS microbiology reviews · 2025Review
- Clues to transcription/replication collision-induced DNA damage: it was RNAP, in the chromosome, with the fork.FEBS letters · 2025Review
- Structural Basis for Dimerization and Activation of UvrD-family Helicases.bioRxiv : the preprint server for biology · 2024Article
- Mycobacterium tuberculosis Ku Stimulates Multi-round DNA Unwinding by UvrD1 Monomers.Journal of molecular biology · 2024Article
- Processing of stalled replication forks in Bacillus subtilis.FEMS microbiology reviews · 2024Review
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- PcrA Dissociates RecA Filaments and the SsbA and RecO Mediators Counterbalance Such Activity.Frontiers in molecular biosciences · 2022Article
- RNA polymerases from low G+C gram-positive bacteria.Transcription · 2021Review
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- Article
- Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD.Nature communications · 2020Article
- Modified nucleoside triphosphates in bacterial research forRSC chemical biology · 2020Article
- UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain.Communications biology · 2020Article
- Interaction with single-stranded DNA-binding protein localizes ribonuclease HI to DNA replication forks and facilitates R-loop removal.Molecular microbiology · 2020Article
- DNA-Unwinding Dynamics of Escherichia coli UvrD Lacking the C-Terminal 40 Amino Acids.Biophysical journal · 2020Article
- The torpedo effect in Bacillus subtilis: RNase J1 resolves stalled transcription complexes.The EMBO journal · 2020Article
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
The PcrA/UvrD helicase functions in multiple pathways that promote bacterial genome stability including the suppression of conflicts between replication and transcription and facilitating the repair of transcribed DNA. The reported ability of PcrA/UvrD to bind and backtrack RNA polymerase (1,2) might be relevant to these functions, but the structural basis for this activity is poorly understood. In this work, we define a minimal RNA polymerase interaction domain in PcrA, and report its crystal structure at 1.5 Å resolution. The domain adopts a Tudor-like fold that is similar to other RNA polymerase interaction domains, including that of the prototype transcription-repair coupling factor Mfd. Removal or mutation of the interaction domain reduces the ability of PcrA/UvrD to interact with and to remodel RNA polymerase complexes in vitro. The implications of this work for our understanding of the role of PcrA/UvrD at the interface of DNA replication, transcription and repair are discussed.
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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.