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

被引：177

作者：

Robinson, Philip J. ^{[1
]}

Trnka, Michael J. ^{[2
]}

Bushnell, David A. ^{[1
]}

Davis, Ralph E. ^{[1
]}

Mattei, Pierre-Jean ^{[1
]}

Burlingame, Alma L. ^{[2
]}

Kornberg, Roger D. ^{[1
]}

机构：

[1] Stanford Univ, Sch Med, Dept Struct Biol, Stanford, CA 94305 USA

[2] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94158 USA

来源：

CELL | 2016年 / 166卷 / 06期

基金：

美国国家科学基金会;

关键词：

C-TERMINAL DOMAIN; GENERAL TRANSCRIPTION; HEAD MODULE; ARCHITECTURE; YEAST; SUBUNIT; PHOSPHORYLATION; VISUALIZATION; DISSOCIATION; REQUIREMENT;

D O I：

10.1016/j.cell.2016.08.050

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1411 / +

页数：27

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