Coordination of dual incision and repair synthesis in human nucleotide excision repair
Open accessAbstract
Nucleotide excision repair (NER) requires the coordinated sequential assembly and actions of the involved proteins at sites of DNA damage. Following damage recognition, dual incision 5' to the lesion by ERCC1-XPF and 3' to the lesion by XPG leads to the removal of a lesion-containing oligonucleotide of about 30 nucleotides. The resulting single-stranded DNA (ssDNA) gap on the undamaged strand is filled in by DNA repair synthesis. Here, we have asked how dual incision and repair synthesis are coordinated in human cells to avoid the exposure of potentially harmful ssDNA intermediates. Using catalytically inactive mutants of ERCC1-XPF and XPG, we show that the 5' incision by ERCC1-XPF precedes the 3' incision by XPG and that the initiation of repair synthesis does not require the catalytic activity of XPG. We propose that a defined order of dual incision and repair synthesis exists in human cells in the form of a 'cut-patch-cut-patch' mechanism. This mechanism may aid the smooth progression through the NER pathway and contribute to genome integrity.
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Most reports agree that NER gap refilling is extremely rapid and tightly coordinated with incision.
“but most reports seem to agree that the refilling is extremely rapid and tightly coordinated with the incision process [49,50]”
From Mind the gap: keeping UV lesions in check (2011) · cites this paper as [49]
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“How long this ssDNA tract is exposed for, before a DNA polyerase refills the gap is not clear, but most reports seem to agree hat the refilling is extremely rapid and tightly coordinated with he incision process [49,50] (see review by Fagbemi et al.”
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- Authors
- Staresincic, L., Fagbemi, A. F., Enzlin, J. H., Gourdin, A. M., Wijgers, N., Dunand‐Sauthier, I., Giglia‐Mari, G., Clarkson, S. G., Vermeulen, W., & Schärer, O. D.
- Affiliations
- Stony Brook University (US)
- University of Zurich (CH)
- Erasmus MC (NL)
- University of Geneva (CH)
- Corresponding author
- Schärer, Orlando D
- Venue
- The EMBO Journal
- Published
- 2009-03-12
- Volume
- 28
- Issue
- 8
- Pages
- 1111-1120
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC2683701
- OpenAlex
- W2128552081
- Cited by
- 287
- References
- 56
- Citations by year
- 2026: 12 · 2025: 16 · 2024: 14 · 2023: 15 · 2022: 11 · 2021: 19 · 2020: 13 · 2019: 17 · 2018: 13 · 2017: 20 · 2016: 12 · 2015: 13 · 2014: 18 · 2013: 20 · 2012: 18
- FWCI
- 9.67
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Academic Commons (Stony Brook University) (submittedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (submittedVersion)
- HAL (submittedVersion)
- SUNY Digital Repository Support (State University of New York System) (submittedVersion)
- Scholarworks@UNIST (Ulsan National Institute of Science and Technology) (submittedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Funders
- National Science Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (100487, 3100A0)
- ZonMw (917-46-364)
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (917-46-364, 912-03-012, 805-47-193)
- National Institutes of Health (CA092584)
- Office of Science (100487)
- National Cancer Institute (CA-092584, P01CA092584)
- National Institute of General Medical Sciences (R01GM080454, GM080454)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- nucleotide excision repair, repair synthesis, XPG, single-stranded DNA, DNA damage recognition, genome stability, catalytically inactive mutant
- MeSH terms
- DNA Excision Repair Protein ERCC-5, Animals, Cell Line, DNA, DNA Damage, DNA Repair, DNA-Binding Proteins, DNA, Single-Stranded, Endonucleases, Humans, Nuclear Proteins, Transcription Factors, Ultraviolet Rays, Proliferating Cell Nuclear Antigen, Catalytic Domain
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