ArticleeLife2021
Analysis of the PcrA-RNA polymerase complex reveals a helicase interaction motif and a role for PcrA/UvrD helicase in the suppression of R-loops.
Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Transient receptor potential vanilloid 2 functions as a directional driver for hepoxilin AScience advances · 2026Article
- Alternative nucleic acid structures in microbial biology: regulatory functions and antimicrobial opportunities.Frontiers in cellular and infection microbiology · 2026Review
- 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
- 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
- Review
- The Impact of RNA-DNA Hybrids on Genome Integrity in Bacteria.Annual review of microbiology · 2022Review
- RNA polymerase pausing, stalling and bypass during transcription of damaged DNA: from molecular basis to functional consequences.Nucleic acids research · 2022Review
- Article
- Alignment of helicases on single-stranded DNA increases activity.Methods in enzymology · 2022Article
- Multiple classes and isoforms of the RNA polymerase recycling motor protein HelD.MicrobiologyOpen · 2021Article
- RNA polymerases from low G+C gram-positive bacteria.Transcription · 2021Review
- Article
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The PcrA/UvrD helicase binds directly to RNA polymerase (RNAP) but the structural basis for this interaction and its functional significance have remained unclear. In this work, we used biochemical assays and hydrogen-deuterium exchange coupled to mass spectrometry to study the PcrA-RNAP complex. We find that PcrA binds tightly to a transcription elongation complex in a manner dependent on protein:protein interaction with the conserved PcrA C-terminal Tudor domain. The helicase binds predominantly to two positions on the surface of RNAP. The PcrA C-terminal domain engages a conserved region in a lineage-specific insert within the β subunit which we identify as a helicase interaction motif present in many other PcrA partner proteins, including the nucleotide excision repair factor UvrB. The catalytic core of the helicase binds near the RNA and DNA exit channels and blocking PcrA activity in vivo leads to the accumulation of R-loops. We propose a role for PcrA as an R-loop suppression factor that helps to minimize conflicts between transcription and other processes on DNA including replication.
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Registered trials
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