ArticleDNA repair2020
A combined structural and biochemical approach reveals translocation and stalling of UvrB on the DNA lesion as a mechanism of damage verification in bacterial nucleotide excision repair.
Article in DNA repair, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- Structural snapshots of the mechanism of ATP-dependent DNA damage recognition by UvrA.Nature communications · 2025Article
- Flavisericum labens gen. nov., sp. nov., a novel member of the family Flavobacteriaceae isolated from the seawater of Dongshan Bay.Antonie van Leeuwenhoek · 2025Article
- Mechanistic understanding of UvrA damage detection and lesion hand-off to UvrB in Nucleotide Excision Repair.Nature communications · 2025Article
- Structural and functional insights into the activation of the dual incision activity of UvrC, a key player in bacterial NER.Nucleic acids research · 2023Article
- Interrogating the substrate specificity landscape of UvrC reveals novel insights into its non-canonical function.Biophysical journal · 2022Article
- Mechanism of transcription modulation by the transcription-repair coupling factor.Nucleic acids research · 2022Article
- Article
- In vitro reconstitution of an efficient nucleotide excision repair system using mesophilic enzymes from Deinococcus radiodurans.Communications biology · 2022Article
- A Peek Inside the Machines of Bacterial Nucleotide Excision Repair.International journal of molecular sciences · 2021Review
- Archaeal DNA Repair Mechanisms.Biomolecules · 2020Review
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Authors and funding
10 authors.
Funding
Abstract
Nucleotide excision repair (NER) is a DNA repair pathway present in all domains of life. In bacteria, UvrA protein localizes the DNA lesion, followed by verification by UvrB helicase and excision by UvrC double nuclease. UvrA senses deformations and flexibility of the DNA duplex without precisely localizing the lesion in the damaged strand, an element essential for proper NER. Using a combination of techniques, we elucidate the mechanism of the damage verification step in bacterial NER. UvrA dimer recruits two UvrB molecules to its two sides. Each of the two UvrB molecules clamps a different DNA strand using its β-hairpin element. Both UvrB molecules then translocate to the lesion, and UvrA dissociates. The UvrB molecule that clamps the damaged strand gets stalled at the lesion to recruit UvrC. This mechanism allows UvrB to verify the DNA damage and identify its precise location triggering subsequent steps in the NER pathway.
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Registered trials
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