Rxivist logo

The complete structure of the human TFIIH core complex

By Basil Greber, Daniel Toso, Jie Fang, Eva Nogales

Posted 28 Dec 2018
bioRxiv DOI: 10.1101/507723 (published DOI: 10.7554/eLife.44771)

Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair. The TFIIH core complex is sufficient for its repair functions and harbors the XPB and XPD DNA-dependent ATPase/helicase subunits, which are affected by human disease mutations. Transcription initiation additionally requires the CdK activating kinase subcomplex. Previous structural work has provided only partial insight into the architecture of TFIIH and its interactions within transcription pre-initiation complexes. Here, we present the complete structure of the human TFIIH core complex, determined by phase-plate cryo-electron microscopy at 3.7 Angstroms resolution. The structure uncovers the molecular basis of TFIIH assembly, revealing how the recruitment of XPB by p52 depends on a pseudo-symmetric dimer of homologous domains in these two proteins. The structure also suggests a function for p62 in the regulation of XPD, and allows the mapping of previously unresolved human disease mutations.

Download data

  • Downloaded 1,081 times
  • Download rankings, all-time:
    • Site-wide: 10,025 out of 88,816
    • In biophysics: 310 out of 3,865
  • Year to date:
    • Site-wide: 45,694 out of 88,816
  • Since beginning of last month:
    • Site-wide: 47,022 out of 88,816

Altmetric data


Downloads over time

Distribution of downloads per paper, site-wide


PanLingua

Sign up for the Rxivist weekly newsletter! (Click here for more details.)


News