ArticleNucleic acids research2020
The TFIIH subunits p44/p62 act as a damage sensor during nucleotide excision repair.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- Integrating Structural, Biochemical, and Cellular Perspectives on the TFIIH Helicases XPB and XPD.Biomolecules · 2026Review
- P62 in colorectal cancer: from inflammation suppression to cancer promotion.Frontiers in immunology · 2026Review
- Review
- p62/SQSTM1 in cancer: phenomena, mechanisms, and regulation in DNA damage repair.Cancer metastasis reviews · 2025Review
- XPD stalled on cross-linked DNA provides insight into damage verification.Nature structural & molecular biology · 2024Article
- Molecular architecture and functional dynamics of the pre-incision complex in nucleotide excision repair.Nature communications · 2024Article
- Interplay of the Tfb1 pleckstrin homology domain with Rad2 and Rad4 in transcription coupled and global genomic nucleotide excision repair.Nucleic acids research · 2024Article
- Characterization of human XPD helicase activity with single-molecule magnetic tweezers.Biophysical journal · 2024Article
- C. elegans TFIIH subunit GTF-2H5/TTDA is a non-essential transcription factor indispensable for DNA repair.Communications biology · 2021Article
- 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
- Editorial: Single-molecule studies of DNA-protein interactions collection 2021.Nucleic acids research · 2021Article
- The Interaction Efficiency of XPD-p44 With Bulky DNA Damages Depends on the Structure of the Damage.Frontiers in cell and developmental biology · 2021Article
- DNA bridges: A novel platform for single-molecule sequencing and other DNA-protein interaction applications.PloS one · 2021Article
- Searching for DNA Damage: Insights From Single Molecule Analysis.Frontiers in molecular biosciences · 2021Review
- Envisioning how the prototypic molecular machine TFIIH functions in transcription initiation and DNA repair.DNA repair · 2020Review
- High-resolution cryo-EM structures of TFIIH and their functional implications.Current opinion in structural biology · 2019Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Nucleotide excision repair (NER) in eukaryotes is orchestrated by the core form of the general transcription factor TFIIH, containing the helicases XPB, XPD and five 'structural' subunits, p62, p44, p34, p52 and p8. Recent cryo-EM structures show that p62 makes extensive contacts with p44 and in part occupies XPD's DNA binding site. While p44 is known to regulate the helicase activity of XPD during NER, p62 is thought to be purely structural. Here, using helicase and adenosine triphosphatase assays we show that a complex containing p44 and p62 enhances XPD's affinity for dsDNA 3-fold over p44 alone. Remarkably, the relative affinity is further increased to 60-fold by dsDNA damage. Direct binding studies show this preference derives from p44/p62's high affinity (20 nM) for damaged ssDNA. Single molecule imaging of p44/p62 complexes without XPD reveals they bind to and randomly diffuse on DNA, however, in the presence of UV-induced DNA lesions these complexes stall. Combined with the analysis of a recent cryo-EM structure, we suggest that p44/p62 acts as a novel DNA-binding entity that enhances damage recognition in TFIIH. This revises our understanding of TFIIH and prompts investigation into the core subunits for an active role during DNA repair and/or transcription.
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Registered trials
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