English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

Architecture of the RNA polymerase II–Mediator core initiation complex.

MPS-Authors
/persons/resource/persons145292

Tegunov,  D.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77721

Baumeister,  W.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78832

Villa,  E.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Plaschka, C., Larivière, L., Wenzeck, L., Seizl, M., Hemann, M., Tegunov, D., et al. (2015). Architecture of the RNA polymerase II–Mediator core initiation complex. Nature, 518, 376-380. doi:10.1038/nature14229.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0025-7671-C
Abstract
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.