ArticleDNA repair2009
The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair.
Article in DNA repair, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
31 citing papers in PubMed, 59 citations in OpenAlex.
- 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
- Advances in the joint profiling technologies of 5mC and 5hmC.RSC chemical biology · 2024Review
- Simultaneous sequencing of genetic and epigenetic bases in DNA.Nature biotechnology · 2023Article
- Article
- Quantitative and kinetic single-molecule analysis of DNA unwinding byBiophysics and physicobiology · 2022Article
- Article
- Roles of the C-Terminal Amino Acids of Non-Hexameric Helicases: Insights fromInternational journal of molecular sciences · 2021Review
- A Peek Inside the Machines of Bacterial Nucleotide Excision Repair.International journal of molecular sciences · 2021Review
- UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain.Communications biology · 2020Article
- DNA-Unwinding Dynamics of Escherichia coli UvrD Lacking the C-Terminal 40 Amino Acids.Biophysical journal · 2020Article
- Rep and UvrD Antagonize One Another at Stalled Replication Forks and This Is Exacerbated by SSB.ACS omega · 2019Article
- Regulation of UvrD Helicase Activity by MutL.Journal of molecular biology · 2018Article
- The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase.Nucleic acids research · 2017Article
- Genome-wide transcription-coupled repair inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- A Magic Spot in Genome Maintenance.Trends in genetics : TIG · 2017Review
- 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
- Genomic survey and expression analysis of DNA repair genes in the genus Leptospira.Molecular genetics and genomics : MGG · 2016Article
- MxiA, MxiC and IpaD Regulate Substrate Selection and Secretion Mode in the T3SS of Shigella flexneri.PloS one · 2016Article
- Active displacement of RecA filaments by UvrD translocase activity.Nucleic acids research · 2015Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
During nucleotide excision repair (NER) in bacteria the UvrC nuclease and the short oligonucleotide that contains the DNA lesion are removed from the post-incision complex by UvrD, a superfamily 1A helicase. Helicases are frequently regulated by interactions with partner proteins, and immunoprecipitation experiments have previously indicated that UvrD interacts with UvrB, a component of the post-incision complex. We examined this interaction using 2-hybrid analysis and surface plasmon resonance spectroscopy, and found that the N-terminal domain and the unstructured region at the C-terminus of UvrD interact with UvrB. We analysed the properties of a truncated UvrD protein that lacked the unstructured C-terminal region and found that it showed a diminished affinity for single-stranded DNA, but retained the ability to displace both UvrC and the lesion-containing oligonucleotide from a post-incision nucleotide excision repair complex. The interaction of the C-terminal region of UvrD with UvrB is therefore not an essential feature of the mechanism by which UvrD disassembles the post-incision complex during NER. In further experiments we showed that PcrA helicase from Bacillus stearothermophilus can also displace UvrC and the excised oligonucleotide from a post-incision NER complex, which supports the idea that PcrA performs a UvrD-like function during NER in gram-positive organisms.
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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.