The complete structure of the human TFIIH core complex

Greber, Basil J.; Toso, Daniel B.; Fang, Jie; Nogales, Eva

doi:10.7554/eLife.44771

Title: The complete structure of the human TFIIH core complex

Journal Article · Tue Mar 12 00:00:00 EDT 2019 · eLife

DOI:https://doi.org/10.7554/eLife.44771· OSTI ID:1571982

^[1]; Toso, Daniel B. ^[2]; Fang, Jie ^[2];

^[1]

Univ. of California, Berkeley, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Univ. of California, Berkeley, CA (United States)

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 Å 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.

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Research Organization:: Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1571982

Journal Information:: eLife, Vol. 8; ISSN 2050-084X

Publisher:: eLife Sciences Publications, Ltd.Copyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 58 works

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DNA Quality Control by a Lesion Sensor Pocket of the Xeroderma Pigmentosum Group D Helicase Subunit of TFIIH Mathieu, Nadine; Kaczmarek, Nina; Rüthemann, Peter Current Biology, Vol. 23, Issue 3 https://doi.org/10.1016/j.cub.2012.12.032	journal	February 2013
Expanding the boundaries of cryo-EM with phase plates Danev, Radostin; Baumeister, Wolfgang Current Opinion in Structural Biology, Vol. 46 https://doi.org/10.1016/j.sbi.2017.06.006	journal	October 2017
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Solution Structure and Self-association Properties of the p8 TFIIH Subunit Responsible for Trichothiodystrophy Vitorino, Marc; Coin, Frédéric; Zlobinskaya, Olga Journal of Molecular Biology, Vol. 368, Issue 2 https://doi.org/10.1016/j.jmb.2007.02.020	journal	April 2007
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