Architecture of the RNA polymerase II-Mediator core initiation complex

The conserved co-activator complex Mediator enables regulated transcription initiation by RNA polymerase (Pol) II. Here we reconstitute an active 15-subunit core Mediator (cMed) comprising all essential Mediator subunits from Saccharomyces cerevisiae. The cryo-electron microscopic structure of cMed...

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Bibliographic Details
Published in:Nature (London) 2015-02, Vol.518 (7539), p.376-380
Main Authors: Plaschka, C, Larivière, L, Wenzeck, L, Seizl, M, Hemann, M, Tegunov, D, Petrotchenko, E V, Borchers, C H, Baumeister, W, Herzog, F, Villa, E, Cramer, P
Format: Article
Language:English
Subjects:
Allosteric Regulation
Binding Sites
Cryoelectron Microscopy
Deoxyribonucleic acid
DNA
DNA - chemistry
DNA - metabolism
Enzyme Activation
Genetic transcription
Kinases
Mediator Complex - chemistry
Mediator Complex - metabolism
Mediator Complex - ultrastructure
Microscopy
Models, Molecular
Phosphorylation
Physiological aspects
Protein research
Protein Stability
Protein Structure, Tertiary
Protein Subunits - chemistry
Protein Subunits - metabolism
RNA polymerase
RNA Polymerase II - chemistry
RNA Polymerase II - metabolism
RNA Polymerase II - ultrastructure
RNA polymerases
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - ultrastructure
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Saccharomyces cerevisiae Proteins - ultrastructure
Transcription Factor TFIIB - chemistry
Transcription Factor TFIIB - metabolism
Transcription Factor TFIIH - chemistry
Transcription Factor TFIIH - metabolism
Transcription factors
Transcription Initiation, Genetic
Yeast
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Summary:The conserved co-activator complex Mediator enables regulated transcription initiation by RNA polymerase (Pol) II. Here we reconstitute an active 15-subunit core Mediator (cMed) comprising all essential Mediator subunits from Saccharomyces cerevisiae. The cryo-electron microscopic structure of cMed bound to a core initiation complex was determined at 9.7 Å resolution. cMed binds Pol II around the Rpb4-Rpb7 stalk near the carboxy-terminal domain (CTD). The Mediator head module binds the Pol II dock and the TFIIB ribbon and stabilizes the initiation complex. The Mediator middle module extends to the Pol II foot with a 'plank' that may influence polymerase conformation. The Mediator subunit Med14 forms a 'beam' between the head and middle modules and connects to the tail module that is predicted to bind transcription activators located on upstream DNA. The Mediator 'arm' and 'hook' domains contribute to a 'cradle' that may position the CTD and TFIIH kinase to stimulate Pol II phosphorylation.
ISSN:0028-0836
1476-4687
DOI:10.1038/nature14229