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TitleThe TFIIH subunits p44/p62 act as a damage sensor during nucleotide excision repair.
Journal, issue, pagesNucleic Acids Res, Vol. 48, Issue 22, Page 12689-12696, Year 2020
Publish dateDec 16, 2020
AuthorsJamie T Barnett / Jochen Kuper / Wolfgang Koelmel / Caroline Kisker / Neil M Kad /
PubMed AbstractNucleotide 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, ...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.
External linksNucleic Acids Res / PubMed:33166411 / PubMed Central
MethodsEM (single particle)
Resolution3.5 Å
Structure data

PDB-7ad8:
Core TFIIH-XPA-DNA complex with modelled p62 subunit
Method: ELECTRON MICROSCOPY / Resolution: 3.5 Å

Chemicals

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

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsDNA BINDING PROTEIN / DNA repair / transcription factor

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