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TitleStructural basis of TFIIH activation for nucleotide excision repair.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 2885, Year 2019
Publish dateJun 28, 2019
AuthorsGoran Kokic / Aleksandar Chernev / Dimitry Tegunov / Christian Dienemann / Henning Urlaub / Patrick Cramer /
PubMed AbstractNucleotide 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 ...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.
External linksNat Commun / PubMed:31253769 / PubMed Central
MethodsEM (single particle)
Resolution3.5 Å
Structure data

4970

6ro4

EMDB-4970, PDB-6ro4:
Structure of the core TFIIH-XPA-DNA complex
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSLOCASE / Complex / Helicase / DNA repair

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