Cited by 435DNA Repair MechanismsDNA and Nucleic Acid ChemistryCarcinogens and Genotoxicity Assessment

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A multistep damage recognition mechanism for global genomic nucleotide excision repair

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Sugasawa, Kaoru, Okamoto, Tomoko, Shimizu, Yuichiro, Masutani, Chikahide, Iwai, Shigenori, Hanaoka, Fumio·2001·Genes & Development

DOI 10.1101/gad.866301PMC PMC312644

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Abstract

A mammalian nucleotide excision repair (NER) factor, the XPC–HR23B complex, can specifically bind to certain DNA lesions and initiate the cell-free repair reaction. Here we describe a detailed analysis of its binding specificity using various DNA substrates, each containing a single defined lesion. A highly sensitive gel mobility shift assay revealed that XPC–HR23B specifically binds a small bubble structure with or without damaged bases, whereas dual incision takes place only when damage is present in the bubble. This is evidence that damage recognition for NER is accomplished through at least two steps; XPC–HR23B first binds to a site that has a DNA helix distortion, and then the presence of injured bases is verified prior to dual incision. Cyclobutane pyrimidine dimers (CPDs) were hardly recognized by XPC–HR23B, suggesting that additional factors may be required for CPD recognition. Although the presence of mismatched bases opposite a CPD potentiated XPC–HR23B binding, probably due to enhancement of the helix distortion, cell-free excision of such compound lesions was much more efficient than expected from the observed affinity for XPC–HR23B. This also suggests that additional factors and steps are required for the recognition of some types of lesions. A multistep mechanism of this sort may provide a molecular basis for ensuring the high level of damage discrimination that is required for global genomic NER.

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3 retracted

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Authors: Sugasawa, K., Okamoto, T., Shimizu, Y., Masutani, C., Iwai, S., & Hanaoka, F.
Affiliations: Japan Science and Technology Agency (JP)
ORCID: Sugasawa, Kaoru
Okamoto, Tomoko
Shimizu, Yuichiro
Masutani, Chikahide
Iwai, Shigenori
Hanaoka, Fumio
Venue: Genes & Development
Publisher: Cold Spring Harbor Laboratory
Published: 2001-03-01
Volume: 15
Issue: 5
Pages: 507-521
ISSN: 0890-9369 (ISSN-L)
1549-5477
DOI: 10.1101/gad.866301
PMC: PMC312644
OpenAlex: W2106443150
Cited by: 435
References: 61
Citations by year: 2026: 10 · 2025: 10 · 2024: 4 · 2023: 14 · 2022: 8 · 2021: 12 · 2020: 12 · 2019: 14 · 2018: 12 · 2017: 18 · 2016: 30 · 2015: 26 · 2014: 16 · 2013: 17 · 2012: 20
Type: posted content
Language: en
Open access: bronze
doi.org
Locations: Genes & Development (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Japan Science and Technology Corporation (CREST)
RIKEN
Core Research for Evolutional Science and Technology
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 › Cancer Research › Carcinogens and Genotoxicity Assessment
Keywords: nucleotide excision repair, DNA damage recognition, helix distortion, cyclobutane pyrimidine dimers
MeSH terms: Deoxyribonuclease I, DNA Damage, DNA Repair, DNA-Binding Proteins, Humans, Models, Biological, Nucleic Acid Conformation, Plasmids, Protein Binding, Pyrimidine Dimers, Tumor Cells, Cultured, Genome, Human, DNA Footprinting, Base Pair Mismatch

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A multistep damage recognition mechanism for global genomic nucleotide excision repair

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