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Architecture of the Mediator head module

Author

Listed:
  • Tsuyoshi Imasaki

    (Indiana University School of Medicine, 635 Barnhill Drive)

  • Guillermo Calero

    (Stanford University School of Medicine
    Present addresses: Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15260, USA (G. Calero); School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, China (G. Cai).)

  • Gang Cai

    (The Scripps Research Institute
    Present addresses: Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15260, USA (G. Calero); School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, China (G. Cai).)

  • 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)

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.

Suggested Citation

  • 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. Asturia, 2011. "Architecture of the Mediator head module," Nature, Nature, vol. 475(7355), pages 240-243, July.
    • Handle: RePEc:nat:nature:v:475:y:2011:i:7355:d:10.1038_nature10162
    DOI: 10.1038/nature10162
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    Cited by:

    1. Theresa Niederberger & Stefanie Etzold & Michael Lidschreiber & Kerstin C Maier & Dietmar E Martin & Holger Fröhlich & Patrick Cramer & Achim Tresch, 2012. "MC EMiNEM Maps the Interaction Landscape of the Mediator," PLOS Computational Biology, Public Library of Science, vol. 8(6), pages 1-10, June.

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