ArticlePloS one2013
The conserved C-terminus of the PcrA/UvrD helicase interacts directly with RNA polymerase.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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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.
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Who cites it
29 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- Mycobacterium tuberculosis Ku Stimulates Multi-round DNA Unwinding by UvrD1 Monomers.Journal of molecular biology · 2024Article
- Pathogenic bacteria experience pervasive RNA polymerase backtracking during infection.bioRxiv : the preprint server for biology · 2023Article
- Dimeric assembly of human Suv3 helicase promotes its RNA unwinding function in mitochondrial RNA degradosome for RNA decay.Protein science : a publication of the Protein Society · 2022Article
- Article
- β-CASP proteins removing RNA polymerase from DNA: when a torpedo is needed to shoot a sitting duck.Nucleic acids research · 2021Review
- Bypass of complex co-directional replication-transcription collisions by replisome skipping.Nucleic acids research · 2021Article
- RNA polymerases from low G+C gram-positive bacteria.Transcription · 2021Review
- Regulation of E. coli Rep helicase activity by PriC.Journal of molecular biology · 2021Article
- Article
- UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain.Communications biology · 2020Article
- Replisome bypass of transcription complexes and R-loops.Nucleic acids research · 2020Article
- Direct removal of RNA polymerase barriers to replication by accessory replicative helicases.Nucleic acids research · 2019Article
- Regulation of UvrD Helicase Activity by MutL.Journal of molecular biology · 2018Article
- Article
- 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
- Understanding bias in DNA repair.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Mfd Protein and Transcription-Repair Coupling in Escherichia coli.Photochemistry and photobiology · 2017Review
- A Magic Spot in Genome Maintenance.Trends in genetics : TIG · 2017Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
UvrD-like helicases play diverse roles in DNA replication, repair and recombination pathways. An emerging body of evidence suggests that their different cellular functions are directed by interactions with partner proteins that target unwinding activity to appropriate substrates. Recent studies in E. coli have shown that UvrD can act as an accessory replicative helicase that resolves conflicts between the replisome and transcription complexes, but the mechanism is not understood. Here we show that the UvrD homologue PcrA interacts physically with B. subtilis RNA polymerase, and that an equivalent interaction is conserved in E. coli where UvrD, but not the closely related helicase Rep, also interacts with RNA polymerase. The PcrA-RNAP interaction is direct and independent of nucleic acids or additional mediator proteins. A disordered but highly conserved C-terminal region of PcrA, which distinguishes PcrA/UvrD from otherwise related enzymes such as Rep, is both necessary and sufficient for interaction with RNA polymerase.
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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.