ArticleNucleic acids research2013
Real-time single-molecule imaging reveals a direct interaction between UvrC and UvrB on DNA tightropes.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Insight into Single-Molecule Imaging Techniques for the Study of Prokaryotic Genome Maintenance.Chemical & biomedical imaging · 2024Review
- Single-molecule analysis of DNA-binding proteins from nuclear extracts (SMADNE).Nucleic acids research · 2023Article
- Structural and functional insights into the activation of the dual incision activity of UvrC, a key player in bacterial NER.Nucleic acids research · 2023Article
- Article
- Interrogating the substrate specificity landscape of UvrC reveals novel insights into its non-canonical function.Biophysical journal · 2022Article
- In vitro reconstitution of an efficient nucleotide excision repair system using mesophilic enzymes from Deinococcus radiodurans.Communications biology · 2022Article
- Single-molecule fluorescence imaging techniques reveal molecular mechanisms underlying deoxyribonucleic acid damage repair.Frontiers in bioengineering and biotechnology · 2022Review
- TIN2 is an architectural protein that facilitates TRF2-mediated trans- and cis-interactions on telomeric DNA.Nucleic acids research · 2021Article
- Single-molecule studies of helicases and translocases in prokaryotic genome-maintenance pathways.DNA repair · 2021Review
- Searching for DNA Damage: Insights From Single Molecule Analysis.Frontiers in molecular biosciences · 2021Review
- The TFIIH subunits p44/p62 act as a damage sensor during nucleotide excision repair.Nucleic acids research · 2020Article
- Tethering-facilitated DNA 'opening' and complementary roles of β-hairpin motifs in the Rad4/XPC DNA damage sensor protein.Nucleic acids research · 2020Article
- UvrC Coordinates an OJournal of the American Chemical Society · 2020Article
- Cohesin SA1 and SA2 are RNA binding proteins that localize to RNA containing regions on DNA.Nucleic acids research · 2020Article
- Guidelines for DNA recombination and repair studies: Mechanistic assays of DNA repair processes.Microbial cell (Graz, Austria) · 2019Review
- Visualizing the Interaction Between the Qdot-labeled Protein and Site-specifically Modified λ DNA at the Single Molecule Level.Journal of visualized experiments : JoVE · 2018Article
- Recruitment of UvrBC complexes to UV-induced damage in the absence of UvrA increases cell survival.Nucleic acids research · 2018Article
- PARP1 changes from three-dimensional DNA damage searching to one-dimensional diffusion after auto-PARylation or in the presence of APE1.Nucleic acids research · 2017Article
- CpG and methylation-dependent DNA binding and dynamics of the methylcytosine binding domain 2 protein at the single-molecule level.Nucleic acids research · 2017Article
- Mechanistic insights into transcription coupled DNA repair.DNA repair · 2017Review
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8 authors.
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Abstract
Nucleotide excision DNA repair is mechanistically conserved across all kingdoms of life. In prokaryotes, this multi-enzyme process requires six proteins: UvrA-D, DNA polymerase I and DNA ligase. To examine how UvrC locates the UvrB-DNA pre-incision complex at a site of damage, we have labeled UvrB and UvrC with different colored quantum dots and quantitatively observed their interactions with DNA tightropes under a variety of solution conditions using oblique angle fluorescence imaging. Alone, UvrC predominantly interacts statically with DNA at low salt. Surprisingly, however, UvrC and UvrB together in solution bind to form the previously unseen UvrBC complex on duplex DNA. This UvrBC complex is highly motile and engages in unbiased one-dimensional diffusion. To test whether UvrB makes direct contact with the DNA in the UvrBC-DNA complex, we investigated three UvrB mutants: Y96A, a β-hairpin deletion and D338N. These mutants affected the motile properties of the UvrBC complex, indicating that UvrB is in intimate contact with the DNA when bound to UvrC. Given the in vivo excess of UvrB and the abundance of UvrBC in our experiments, this newly identified complex is likely to be the predominant form of UvrC in the cell.
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