Structures of transcription pre-initiation complex with TFIIH and Mediator

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 resol...

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Vydáno v:	Nature (London) Ročník 551; číslo 7679; s. 204 - 209
Hlavní autoři:	Schilbach, S., Hantsche, M., Tegunov, D., Dienemann, C., Wigge, C., Urlaub, H., Cramer, P.
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	London Nature Publishing Group UK 09.11.2017 Nature Publishing Group
Témata:	13/109 14/28 631/1647/296 631/337/572 631/45/147 631/535/1258/1259 631/92/607/1167 82/58 82/80 82/83 Analysis Brewer's yeast Coordination compounds Cryoelectron Microscopy Deoxyribonucleic acid DNA DNA - chemistry DNA - genetics DNA - metabolism DNA binding proteins DNA repair DNA-directed RNA polymerase Electron microscopy Genetic aspects Genetic transcription Homology Humanities and Social Sciences Identification and classification Initiation complex Kinases Mediator Complex - chemistry Mediator Complex - metabolism Mediator Complex - ultrastructure Microscopy Models, Molecular multidisciplinary Observations Open spaces Phosphorylation Promoter Regions, Genetic Protein Binding Protein Subunits - chemistry Protein Subunits - metabolism Proteins Ribonucleic acid RNA RNA polymerase II RNA Polymerase II - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Saccharomyces cerevisiae Proteins - ultrastructure Science Structure Transcription (Genetics) Transcription factors Transcription Factors, TFII - chemistry Transcription Factors, TFII - metabolism Transcription Factors, TFII - ultrastructure Transcription Initiation, Genetic Yeast Germany
ISSN:	0028-0836, 1476-4687, 1476-4687
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Popis
Shrnutí:	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. Cryo-electron microscopy structures of the yeast pre-initiation complex (PIC) and its complex with core Mediator provide insights into the opening of promoter DNA and the initiation of transcription. TFIIH in the transcription pre-initiation complex To initiate gene transcription, RNA polymerase (Pol) II assembles with general transcription factors on promoter DNA to form the pre-initiation complex (PIC). Here, Patrick Cramer and colleagues describe cryo-electron microscopy structures of the yeast PIC and the PIC bound to the core Mediator (cMed) complex. The latter structure with the general coactivator Mediator has 46 factors, including all those that are essential for transcription initiation in yeast. The structures reveal the architecture of transcription factor IIH (TFIIH) and suggest how its 'core' and 'kinase' modules might function in promoter opening and Pol II phosphorylation, respectively.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ISSN:	0028-0836 1476-4687 1476-4687
DOI:	10.1038/nature24282