| Literature DB >> 27610567 |
Philip J Robinson1, Michael J Trnka2, David A Bushnell1, Ralph E Davis1, Pierre-Jean Mattei1, Alma L Burlingame2, Roger D Kornberg3.
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.Entities:
Keywords: Mediator complex; Pre-initiation complex; RNA polymerase II carboxy-terminal domain; TFIIH; TFIIK; Transcription; cross-linking; cryo-EM; mass spectrometry
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Year: 2016 PMID: 27610567 PMCID: PMC5589196 DOI: 10.1016/j.cell.2016.08.050
Source DB: PubMed Journal: Cell ISSN: 0092-8674 Impact factor: 41.582