ArticleThe Journal of biological chemistry2012
Multiple DNA binding domains mediate the function of the ERCC1-XPF protein in nucleotide excision repair.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- Nucleotide excision repair and poly(ADP-ribose) polymerase 1 cooperate in HBV cccDNA synthesis: A potential viral therapeutic target.JHEP reports : innovation in hepatology · 2026Article
- The interaction of XPG with TFIIH through p62 and XPD is required for the completion of nucleotide excision repair.Nucleic acids research · 2026Article
- Review
- A novel algorithm for the virtual screening of extensive small molecule libraries against ERCC1/XPF protein-protein interaction for the identification of resistance-bypassing potential anticancer molecules.Turkish journal of biology = Turk biyoloji dergisi · 2024Article
- Mechanism of action of nucleotide excision repair machinery.Biochemical Society transactions · 2022Review
- Every protagonist has a sidekick: Structural aspects of human xeroderma pigmentosum-binding proteins in nucleotide excision repair.Protein science : a publication of the Protein Society · 2021Review
- ERCC1-XPF targeting to psoralen-DNA crosslinks depends on XPA and FANCD2.Cellular and molecular life sciences : CMLS · 2020Article
- Deficiency of nucleotide excision repair is associated with mutational signature observed in cancer.Genome research · 2019Article
- Functional Comparison of XPF Missense Mutations Associated to Multiple DNA Repair Disorders.Genes · 2019Article
- Repair protein persistence at DNA lesions characterizes XPF defect with Cockayne syndrome features.Nucleic acids research · 2018Article
- Coordination of Rad1-Rad10 interactions with Msh2-Msh3, Saw1 and RPA is essential for functional 3' non-homologous tail removal.Nucleic acids research · 2018Article
- Distinct roles of XPF-ERCC1 and Rad1-Rad10-Saw1 in replication-coupled and uncoupled inter-strand crosslink repair.Nature communications · 2018Article
- ERCC4 variants identified in a cohort of patients with segmental progeroid syndromes.Human mutation · 2018Article
- Recruitment and positioning determine the specific role of the XPF-ERCC1 endonuclease in interstrand crosslink repair.The EMBO journal · 2017Article
- Single-stranded DNA Binding by the Helix-Hairpin-Helix Domain of XPF Protein Contributes to the Substrate Specificity of the ERCC1-XPF Protein Complex.The Journal of biological chemistry · 2017Article
- Association between XRCC1 and ERCC1 single-nucleotide polymorphisms and the efficacy of concurrent radiochemotherapy in patients with esophageal squamous cell carcinoma.Oncology letters · 2017Article
- Maintenance of genome stability by Fanconi anemia proteins.Cell & bioscience · 2017Review
- Convergence of The Nobel Fields of Telomere Biology and DNA Repair.Photochemistry and photobiology · 2017Review
- Review
- Cell-autonomous progeroid changes in conditional mouse models for repair endonuclease XPG deficiency.PLoS genetics · 2014Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
ERCC1-XPF is a heterodimeric, structure-specific endonuclease that cleaves single-stranded/double-stranded DNA junctions and has roles in nucleotide excision repair (NER), interstrand crosslink (ICL) repair, homologous recombination, and possibly other pathways. In NER, ERCC1-XPF is recruited to DNA lesions by interaction with XPA and incises the DNA 5' to the lesion. We studied the role of the four C-terminal DNA binding domains in mediating NER activity and cleavage of model substrates. We found that mutations in the helix-hairpin-helix domain of ERCC1 and the nuclease domain of XPF abolished cleavage activity on model substrates. Interestingly, mutations in multiple DNA binding domains were needed to significantly diminish NER activity in vitro and in vivo, suggesting that interactions with proteins in the NER incision complex can compensate for some defects in DNA binding. Mutations in DNA binding domains of ERCC1-XPF render cells more sensitive to the crosslinking agent mitomycin C than to ultraviolet radiation, suggesting that the ICL repair function of ERCC1-XPF requires tighter substrate binding than NER. Our studies show that multiple domains of ERCC1-XPF contribute to substrate binding, and are consistent with models of NER suggesting that multiple weak protein-DNA and protein-protein interactions drive progression through the pathway. Our findings are discussed in the context of structural studies of individual domains of ERCC1-XPF and of its role in multiple DNA repair pathways.
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