ArticleNucleic acids research2017
The intricate network between the p34 and p44 subunits is central to the activity of the transcription/DNA repair factor TFIIH.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 24 citations in OpenAlex.
- Review
- XPD stalled on cross-linked DNA provides insight into damage verification.Nature structural & molecular biology · 2024Article
- Characterization of human XPD helicase activity with single-molecule magnetic tweezers.Biophysical journal · 2024Article
- A Time and Cost-Effective Pipeline for Expression Screening and Protein Production in Insect Cells Based on the HR-Bac Toolbox to Generate Recombinant Baculoviruses.Methods in molecular biology (Clifton, N.J.) · 2024Article
- HR-Bac, a toolbox based on homologous recombination for expression, screening and production of multiprotein complexes using the baculovirus expression system.Scientific reports · 2022Article
- Insect Cells-Baculovirus System for the Production of Difficult to Express Proteins: From Expression Screening for Soluble Constructs to Protein Quality Control.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The structure of the cysteine-rich region from human histone-lysine N-methyltransferase EHMT2 (G9a).Journal of structural biology: X · 2021Article
- The TFIIH subunits p44/p62 act as a damage sensor during nucleotide excision repair.Nucleic acids research · 2020Article
- How to limit the speed of a motor: the intricate regulation of the XPB ATPase and translocase in TFIIH.Nucleic acids research · 2020Article
- Structural basis of TFIIH activation for nucleotide excision repair.Nature communications · 2019Article
- Transcription preinitiation complex structure and dynamics provide insight into genetic diseases.Nature structural & molecular biology · 2019Article
- Article
- The essential and multifunctional TFIIH complex.Protein science : a publication of the Protein Society · 2018Review
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The general transcription factor IIH (TFIIH) is a multi-protein complex and its 10 subunits are engaged in an intricate protein-protein interaction network critical for the regulation of its transcription and DNA repair activities that are so far little understood on a molecular level. In this study, we focused on the p44 and the p34 subunits, which are central for the structural integrity of core-TFIIH. We solved crystal structures of a complex formed by the p34 N-terminal vWA and p44 C-terminal zinc binding domains from Chaetomium thermophilum and from Homo sapiens. Intriguingly, our functional analyses clearly revealed the presence of a second interface located in the C-terminal zinc binding region of p34, which can rescue a disrupted interaction between the p34 vWA and the p44 RING domain. In addition, we demonstrate that the C-terminal zinc binding domain of p34 assumes a central role with respect to the stability and function of TFIIH. Our data reveal a redundant interaction network within core-TFIIH, which may serve to minimize the susceptibility to mutational impairment. This provides first insights why so far no mutations in the p34 or p44 TFIIH-core subunits have been identified that would lead to the hallmark nucleotide excision repair syndromes xeroderma pigmentosum or trichothiodystrophy.
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