Cited by 500DNA Repair MechanismsDNA and Nucleic Acid ChemistryNuclear Structure and Function

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Mechanism of open complex and dual incision formation by human nucleotide excision repair factors

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Evans, Elizabeth, Moggs, Jonathan G., Hwang, Jae R., Egly, Jean‐Marc, Wood, Richard D.·1997·The EMBO Journal

DOI 10.1093/emboj/16.21.6559PMC PMC1170260

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Abstract

During nucleotide excision repair in human cells, a damaged DNA strand is cleaved by two endonucleases, XPG on the 3' side of the lesion and ERCC1-XPF on the 5' side. These structure-specific enzymes act at junctions between duplex and single-stranded DNA. ATP-dependent formation of an open DNA structure of approximately 25 nt around the adduct precedes this dual incision. We investigated the mechanism of open complex formation and find that mutations in XPB or XPD, the DNA helicase subunits of the transcription and repair factor TFIIH, can completely prevent opening and dual incision in cell-free extracts. A deficiency in XPC protein also prevents opening. The absence of RPA, XPA or XPG activities leads to an intermediate level of strand separation. In contrast, XPF or ERCC1-defective extracts open normally and generate a 3' incision, but fail to form the 5' incision. This same repair defect was observed in extracts from human xeroderma pigmentosum cells with an alteration in the C-terminal domain of XPB, suggesting that XPB has an additional role in facilitating 5' incision by ERCC1-XPF nuclease. These data support a mechanism in which TFIIH-associated helicase activity and XPC protein catalyze initial formation of the key open intermediate, with full extension to the cleavage sites promoted by the other core nucleotide excision repair factors. Opening is followed by dual incision, with the 3' cleavage made first.

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Authors: Evans, E., Moggs, J. G., Hwang, J. R., Egly, J., & Wood, R. D.
Affiliations: Institut de génétique et de biologie moléculaire et cellulaire (FR)
Corresponding author: Evans, Elizabeth
ORCID: Evans, Elizabeth
Egly, Jean‐Marc
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1997-11-01
Volume: 16
Issue: 21
Pages: 6559-6573
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1093/emboj/16.21.6559
PMC: PMC1170260
OpenAlex: W2044000184
Cited by: 500
References: 51
Citations by year: 2026: 9 · 2025: 6 · 2024: 11 · 2023: 12 · 2022: 4 · 2021: 12 · 2020: 13 · 2019: 12 · 2018: 10 · 2017: 9 · 2016: 16 · 2015: 18 · 2014: 14 · 2013: 11 · 2012: 16
FWCI: 6.52
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Israel Cancer Research Fund
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: nucleotide excision repair, open complex formation, XPG, TFIIH, XPB helicase, XPC, XPD, XPA, RPA, DNA helicase, DNA strand separation, xeroderma pigmentosum, DNA damage response
MeSH terms: DNA Excision Repair Protein ERCC-5, Adenosine Triphosphate, Cells, Cultured, Cisplatin, DNA, DNA Damage, DNA Repair, DNA Helicases, DNA-Binding Proteins, DNA, Single-Stranded, Endonucleases, HeLa Cells, Humans, Models, Genetic, Nuclear Proteins, DNA Ligases, Proteins, Substrate Specificity, Transcription Factors, Transcription, Genetic, Xeroderma Pigmentosum, Point Mutation, Transcription Factors, TFII, Macromolecular Substances, Replication Protein A, Transcription Factor TFIIH, Xeroderma Pigmentosum Group D Protein, Xeroderma Pigmentosum Group A Protein

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Mechanism of open complex and dual incision formation by human nucleotide excision repair factors

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