Architecture of the Mediator head module

Tsuyoshi Imasaki, Guillermo Calero, Gang Cai, Kuang-Lei Tsai, Kentaro Yamada, Francesco Cardelli, Hediye Erdjument-Bromage, Paul Tempst, Imre Berger, Guy Lorch Kornberg, Francisco J. Asturias, Roger D. Kornberg and Yuichiro Takagi ()
Additional contact information
Tsuyoshi Imasaki: Indiana University School of Medicine, 635 Barnhill Drive
Guillermo Calero: Stanford University School of Medicine
Gang Cai: The Scripps Research Institute
Kuang-Lei Tsai: The Scripps Research Institute
Kentaro Yamada: Indiana University School of Medicine, 635 Barnhill Drive
Francesco Cardelli: Indiana University School of Medicine, 635 Barnhill Drive
Hediye Erdjument-Bromage: Molecular Biology Program, Memorial Sloan-Kettering Cancer Center
Paul Tempst: Molecular Biology Program, Memorial Sloan-Kettering Cancer Center
Imre Berger: European Molecular Biology Laboratory, Grenoble Outstation, 6 rue Jules Horowitz
Guy Lorch Kornberg: Stanford University School of Medicine
Francisco J. Asturias: The Scripps Research Institute
Roger D. Kornberg: Stanford University School of Medicine
Yuichiro Takagi: Indiana University School of Medicine, 635 Barnhill Drive

Nature, 2011, vol. 475, issue 7355, 240-243

Abstract: Mediator gets a head The Mediator complex is a large molecular machine linking transcriptional activators and repressors to RNA polymerase II. It contains three subcomplexes, one of which is a seven-subunit head module. Imasaki et al. have solved the crystallographic structure of the Mediator head module from the yeast Saccharomyces cerevisiae. The subunits form a stable assembly with recognizable binding sites for transcription accessory factors and RNA polymerase II. The structure suggests how transcription factor IIH and the polymerase C-terminal domain are aligned to facilitate phosphorylation of the latter.

Date: 2011
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DOI: 10.1038/nature10162

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