Structural basis of TFIIH activation for nucleotide excision repair
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Abstract
Nucleotide excision repair (NER) is the major DNA repair pathway that removes UV-induced and bulky DNA lesions. There is currently no structure of NER intermediates, which form around the large multisubunit transcription factor IIH (TFIIH). Here we report the cryo-EM structure of an NER intermediate containing TFIIH and the NER factor XPA. Compared to its transcription conformation, the TFIIH structure is rearranged such that its ATPase subunits XPB and XPD bind double- and single-stranded DNA, consistent with their translocase and helicase activities, respectively. XPA releases the inhibitory kinase module of TFIIH, displaces a ‘plug’ element from the DNA-binding pore in XPD, and together with the NER factor XPG stimulates XPD activity. Our results explain how TFIIH is switched from a transcription to a repair factor, and provide the basis for a mechanistic analysis of the NER pathway.
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Placing the Rad14-Rad33 model into a cryo-EM map comprising XPA (Rad14) and TFIIH bound to DNA suggests how the Rad14 C-terminus interacts with TFIIH.
“Placing this model into a cryo EM map comprising XPA (Rad14) and TFIIH bound to DNA (39) suggests how the Rad14 C-terminus, which fits into previously unmodeled density, interacts with TFIIH.”
From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [39]
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- Authors
- Kokic, G., Chernev, A., Tegunov, D., Dienemann, C., Urlaub, H., & Cramer, P.
- Affiliations
- Universitätsmedizin Göttingen (DE)
- Max Planck Institute for Biophysical Chemistry (DE)
- Corresponding author
- Cramer, Patrick
- ORCID
- Venue
- Nature Communications
- Published
- 2019-06-28
- Volume
- 10
- Issue
- 1
- Pages
- 2885-2885
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC6599211
- OpenAlex
- W2953821629
- Cited by
- 163
- References
- 69
- Citations by year
- 2026: 22 · 2025: 17 · 2024: 22 · 2023: 23 · 2022: 18 · 2021: 25 · 2020: 30 · 2019: 6
- FWCI
- 6.53
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (submittedVersion, cc-by)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- Funders
- Deutsche Forschungsgemeinschaft (SFB860, SPP1935)
- Volkswagen Foundation
- European Research Council Advanced Investigator Grant TRANSREGULON
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- nucleotide excision repair, TFIIH, XPA, XPD, XPB, XPG, DNA repair intermediates, helicase activity, UV-induced DNA damage, bulky DNA lesions, cryo-EM structure, transcription factors
- MeSH terms
- DNA Excision Repair Protein ERCC-5, Adenosine Triphosphatases, Animals, Cell Line, Cloning, Molecular, DNA, DNA Repair, DNA Helicases, DNA-Binding Proteins, Endonucleases, Escherichia coli, Gene Expression Regulation, Humans, Insecta, Models, Chemical, Nuclear Proteins, Recombinant Proteins, Transcription Factors, Cryoelectron Microscopy, Transcription Factor TFIIH, Xeroderma Pigmentosum Group D Protein, Xeroderma Pigmentosum Group A Protein
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