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Structure of a Complete Mediator-RNA Polymerase II Pre-Initiation Complex
Author(s) -
Philip J. Robinson,
Michael J. Trnka,
David Bushnell,
Ralph Davis,
PierreJean Matteï,
Alma L. Burlingame,
Roger D. Kornberg
Publication year - 2016
Publication title -
cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 26.304
H-Index - 776
eISSN - 1097-4172
pISSN - 0092-8674
DOI - 10.1016/j.cell.2016.08.050
Subject(s) - biology , mediator , rna polymerase ii , polymerase , genetics , rna polymerase , microbiology and biotechnology , computational biology , rna , dna , gene , gene expression , promoter
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.

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