ArticleCommunications biology2020
UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain.
Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Genetic analysis of epistasis between nucleotide excision repair and homologous recombination in the recovery of persisters after fluoroquinolone treatment.PLoS genetics · 2026Article
- Predicting the protein interaction landscape of a free-living bacterium with pooled-AlphaFold3.Molecular systems biology · 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
- 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
- Thumb-domain dynamics modulate the functional repertoire of DNA-Polymerase IV (DinB).Nucleic acids research · 2023Article
- Recipient UvrD helicase is involved in single- to double-stranded DNA conversion during conjugative plasmid transfer.Nucleic acids research · 2023Article
- Defeating a superbug: A breakthrough in vaccine design against multidrug-resistant Pseudomonas aeruginosa using reverse vaccinology.PloS one · 2023Article
- Article
- Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins.STAR protocols · 2021Article
- Searching for Biological Function of the Mysterious PA2504 Protein fromInternational journal of molecular sciences · 2021Article
- Regulation of E. coli Rep helicase activity by PriC.Journal of molecular biology · 2021Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors.
Funding
Abstract
All living organisms have to cope with the constant threat of genome damage by UV light and other toxic reagents. To maintain the integrity of their genomes, organisms developed a variety of DNA repair pathways. One of these, the Transcription Coupled DNA-Repair (TCR) pathway, is triggered by stalled RNA Polymerase (RNAP) complexes at DNA damage sites on actively transcribed genes. A recently elucidated bacterial TCR pathway employs the UvrD helicase pulling back stalled RNAP complexes from the damage, stimulating recruitment of the DNA-repair machinery. However, structural and functional aspects of UvrD's interaction with RNA Polymerase remain elusive. Here we used advanced solution NMR spectroscopy to investigate UvrD's role within the TCR, identifying that the carboxy-terminal region of the UvrD helicase facilitates RNAP interactions by adopting a Tudor-domain like fold. Subsequently, we functionally analyzed this domain, identifying it as a crucial component for the UvrD-RNAP interaction besides having nucleic-acid affinity.
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