ArticleNucleic acids research2012
Fluorescence-based incision assay for human XPF-ERCC1 activity identifies important elements of DNA junction recognition.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.
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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
15 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Polymorphisms in ERCC4 and ERCC5 and risk of cancers: Systematic research synopsis, meta-analysis, and epidemiological evidence.Frontiers in oncology · 2022Pooled it
- Analysis of cytosine deamination events in excision repair sequencing reads reveals mechanisms of incision site selection in NER.Nucleic acids research · 2024Article
- Repurposing Antimalarial Pyronaridine as a DNA Repair Inhibitor to Exploit the Full Potential of Gold-Nanoparticle-Mediated Radiation Response.Pharmaceutics · 2022Article
- Modulation of ERCC1-XPF Heterodimerization InhibitionFrontiers in oncology · 2022Article
- Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation.Nature communications · 2020Article
- Coordination of Rad1-Rad10 interactions with Msh2-Msh3, Saw1 and RPA is essential for functional 3' non-homologous tail removal.Nucleic acids research · 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
- A rapid method for detecting protein-nucleic acid interactions by protein induced fluorescence enhancement.Scientific reports · 2016Article
- AKAP12 mediates PKA-induced phosphorylation of ATR to enhance nucleotide excision repair.Nucleic acids research · 2016Article
- SUMO-mediated regulation of DNA damage repair and responses.Trends in biochemical sciences · 2015Review
- Sumoylation of the Rad1 nuclease promotes DNA repair and regulates its DNA association.Nucleic acids research · 2014Article
- Mouse SLX4 is a tumor suppressor that stimulates the activity of the nuclease XPF-ERCC1 in DNA crosslink repair.Molecular cell · 2014Article
- XPF-673C>T polymorphism effect on the susceptibility to esophageal cancer in Chinese population.PloS one · 2014Article
- DNA repair endonuclease ERCC1-XPF as a novel therapeutic target to overcome chemoresistance in cancer therapy.Nucleic acids research · 2012Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The structure-specific endonuclease activity of the human XPF-ERCC1 complex is essential for a number of DNA processing mechanisms that help to maintain genomic integrity. XPF-ERCC1 cleaves DNA structures such as stem-loops, bubbles or flaps in one strand of a duplex where there is at least one downstream single strand. Here, we define the minimal substrate requirements for cleavage of stem-loop substrates allowing us to develop a real-time fluorescence-based assay to measure endonuclease activity. Using this assay, we show that changes in the sequence of the duplex upstream of the incision site results in up to 100-fold variation in cleavage rate of a stem-loop substrate by XPF-ERCC1. XPF-ERCC1 has a preference for cleaving the phosphodiester bond positioned on the 3'-side of a T or a U, which is flanked by an upstream T or U suggesting that a T/U pocket may exist within the catalytic domain. In addition to an endonuclease domain and tandem helix-hairpin-helix domains, XPF has a divergent and inactive DEAH helicase-like domain (HLD). We show that deletion of HLD eliminates endonuclease activity and demonstrate that purified recombinant XPF-HLD shows a preference for binding stem-loop structures over single strand or duplex alone, suggesting a role for the HLD in initial structure recognition. Together our data describe features of XPF-ERCC1 and an accepted model substrate that are important for recognition and efficient incision activity.
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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.