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TitleVisualization of stepwise derepression of TFIIH in global genome nucleotide excision repair.
Journal, issue, pagesSci Adv, Vol. 12, Issue 30, Page eaeb3506, Year 2026
Publish dateJul 24, 2026
AuthorsNatàlia de Martín Garrido / Callum A F Haste / Junjie Feng / Nora B Cronin / Basil J Greber /
PubMed AbstractNucleotide excision repair (NER) is a crucial DNA repair pathway that is orchestrated by transcription factor IIH (TFIIH) in eukaryotic cells. TFIIH is a multifunctional complex that contains two DNA ...Nucleotide excision repair (NER) is a crucial DNA repair pathway that is orchestrated by transcription factor IIH (TFIIH) in eukaryotic cells. TFIIH is a multifunctional complex that contains two DNA helicase/DNA translocase subunits and a kinase module, different subsets of which act in NER, transcription initiation, and cell cycle control. To ensure fidelity despite multifunctionality, the DNA helicase activity of TFIIH is autoinhibited in its free form or when the factor engages in transcription initiation. While the release of the kinase module has been identified as a key step in TFIIH activation, the molecular mechanisms controlling this step and concomitant structural changes in TFIIH are incompletely understood. Here, we determine high-resolution structures of three NER intermediates that visualize how TFIIH arrives at sites of DNA damage in an autoinhibited state and how autoinhibition is released via previously undescribed intermediates. These findings contribute to a mechanistic understanding of human DNA repair.
External linksSci Adv / PubMed:42490432 / PubMed Central
MethodsEM (single particle)
Resolution3.29 - 4.6 Å
Structure data

56544

28jm

EMDB-56544, PDB-28jm:
Cryo-EM structure of the human holo-TFIIH and XPC initial encounter complex
Method: EM (single particle) / Resolution: 3.29 Å

56551

28js

EMDB-56551, PDB-28js:
Cryo-EM structure of the human holo-TFIIH-XPC complex bound to bulky lesion-mimic DNA (composite map)
Method: EM (single particle) / Resolution: 3.32 Å

EMDB-56553: Multi-body refinement component 1 of the cryo-EM structure of the human holo-TFIIH-XPC complex bound to bulky lesion-mimic DNA
Method: EM (single particle) / Resolution: 3.5 Å

56566

28jv

EMDB-56566, PDB-28jv:
Cryo-EM structure of the human holo-TFIIH-XPC complex bound to bulky lesion-mimic DNA (consensus map)
Method: EM (single particle) / Resolution: 3.91 Å

EMDB-56568: Multi-body refinement component 2 of the cryo-EM structure of the human holo-TFIIH-XPC complex bound to bulky lesion-mimic DNA
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-56572: Multi-body refinement component 3 of the cryo-EM structure of the human holo-TFIIH-XPC complex bound to bulky lesion-mimic DNA
Method: EM (single particle) / Resolution: 4.6 Å

56573

28ke

EMDB-56573, PDB-28ke:
Cryo-EM structure of the human holo-TFIIH-XPC-XPA complex bound to bulky lesion-mimic DNA
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-ZN:
Unknown entry

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsDNA BINDING PROTEIN / Nucleotide excision repair / DNA Repair / helicase / transcription factor

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