5OQM

STRUCTURE OF YEAST TRANSCRIPTION PRE-INITIATION COMPLEX WITH TFIIH AND CORE MEDIATOR

Summary for 5OQM

• Entry DOI: 10.2210/pdb5oqm/pdb
• Related: 5OQJ
• EMDB information: 3850
• Descriptor: DNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11, ... (49 entities in total)
• Functional Keywords: transcription initiation, transcription, macromolecular complex
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 46
• Total formula weight: 1811060.21

Authors

Schilbach, S.,Hantsche, M.,Tegunov, D.,Dienemann, C.,Wigge, C.,Urlaub, H.,Cramer, P. (deposition date: 2017-08-13, release date: 2018-05-09, Last modification date: 2024-05-15)

Primary citation

Schilbach, S.,Hantsche, M.,Tegunov, D.,Dienemann, C.,Wigge, C.,Urlaub, H.,Cramer, P.
Structures of transcription pre-initiation complex with TFIIH and Mediator.
Nature, 551:204-209, 2017

PubMed Abstract: For the initiation of transcription, RNA polymerase II (Pol II) assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). Here we report cryo-electron microscopy structures of the Saccharomyces cerevisiae PIC and PIC-core Mediator complex at nominal resolutions of 4.7 Å and 5.8 Å, respectively. The structures reveal transcription factor IIH (TFIIH), and suggest how the core and kinase TFIIH modules function in the opening of promoter DNA and the phosphorylation of Pol II, respectively. The TFIIH core subunit Ssl2 (a homologue of human XPB) is positioned on downstream DNA by the 'E-bridge' helix in TFIIE, consistent with TFIIE-stimulated DNA opening. The TFIIH kinase module subunit Tfb3 (MAT1 in human) anchors the kinase Kin28 (CDK7), which is mobile in the PIC but preferentially located between the Mediator hook and shoulder in the PIC-core Mediator complex. Open spaces between the Mediator head and middle modules may allow access of the kinase to its substrate, the C-terminal domain of Pol II.

PubMed: 29088706
DOI: 10.1038/nature24282

Experimental method

ELECTRON MICROSCOPY (5.8 Å)