Format

Send to

Choose Destination
Cell. 2016 Sep 8;166(6):1411-1422.e16. doi: 10.1016/j.cell.2016.08.050.

Structure of a Complete Mediator-RNA Polymerase II Pre-Initiation Complex.

Author information

1
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
2
Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94158, USA.
3
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA. Electronic address: kornberg@stanford.edu.

Abstract

A complete, 52-protein, 2.5 million dalton, Mediator-RNA polymerase II pre-initiation complex (Med-PIC) was assembled and analyzed by cryo-electron microscopy and by chemical cross-linking and mass spectrometry. The resulting complete Med-PIC structure reveals two components of functional significance, absent from previous structures, a protein kinase complex and the Mediator-activator interaction region. It thereby shows how the kinase and its target, the C-terminal domain of the polymerase, control Med-PIC interaction and transcription.

KEYWORDS:

Mediator complex; Pre-initiation complex; RNA polymerase II carboxy-terminal domain; TFIIH; TFIIK; Transcription; cross-linking; cryo-EM; mass spectrometry

PMID:
27610567
PMCID:
PMC5589196
DOI:
10.1016/j.cell.2016.08.050
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center