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Cooperative binding of two acetylation marks on a histone tail by a single bromodomain

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  • Jeanne Morinière

    (European Molecular Biology Laboratory, Grenoble Outstation, 6 rue Jules Horowitz, BP 181, 38042 Grenoble Cedex 9, France
    Unit of Virus Host-Cell Interactions, UMI 3265 Université Joseph Fourier-EMBL-CNRS, 6 rue Jules Horowitz, BP 181, 38042 Grenoble Cedex 9, France)

  • Sophie Rousseaux

    (INSERM, U823
    Université Joseph Fourier, Institut Albert Bonniot)

  • Ulrich Steuerwald

    (European Molecular Biology Laboratory, Meyerhofstrasse 1)

  • Montserrat Soler-López

    (European Molecular Biology Laboratory, Grenoble Outstation, 6 rue Jules Horowitz, BP 181, 38042 Grenoble Cedex 9, France
    Unit of Virus Host-Cell Interactions, UMI 3265 Université Joseph Fourier-EMBL-CNRS, 6 rue Jules Horowitz, BP 181, 38042 Grenoble Cedex 9, France
    Present address: Institute for Research in Biomedicine (IRB Barcelona), Parc Científic de Barcelona, calle Baldiri Reixac 10–12, 08028 Barcelona, Spain.)

  • Sandrine Curtet

    (INSERM, U823
    Université Joseph Fourier, Institut Albert Bonniot)

  • Anne-Laure Vitte

    (INSERM, U823
    Université Joseph Fourier, Institut Albert Bonniot)

  • Jérôme Govin

    (INSERM, U823
    Université Joseph Fourier, Institut Albert Bonniot)

  • Jonathan Gaucher

    (INSERM, U823
    Université Joseph Fourier, Institut Albert Bonniot)

  • Karin Sadoul

    (INSERM, U823
    Université Joseph Fourier, Institut Albert Bonniot)

  • Darren J. Hart

    (European Molecular Biology Laboratory, Grenoble Outstation, 6 rue Jules Horowitz, BP 181, 38042 Grenoble Cedex 9, France
    Unit of Virus Host-Cell Interactions, UMI 3265 Université Joseph Fourier-EMBL-CNRS, 6 rue Jules Horowitz, BP 181, 38042 Grenoble Cedex 9, France)

  • Jeroen Krijgsveld

    (European Molecular Biology Laboratory, Meyerhofstrasse 1)

  • Saadi Khochbin

    (INSERM, U823
    Université Joseph Fourier, Institut Albert Bonniot)

  • Christoph W. Müller

    (European Molecular Biology Laboratory, Meyerhofstrasse 1)

  • Carlo Petosa

    (Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5075 CEA-CNRS-Université Joseph Fourier, 41 Jules Horowitz, 38027 Grenoble Cedex 1, France)

Abstract

Histone modification: tail spin Brdt1 is a bromodomain-containing chromatin protein that can compact hyperacetylated chromatin and has important functions during spermiogenesis. Here, the crystal structure of a bromodomain of Brdt1 bound to an acetylated histone H4 tail reveals a combinatorial mode of binding to post-translational modifications where a single effector module engages two marks on a histone tail.

Suggested Citation

  • Jeanne Morinière & Sophie Rousseaux & Ulrich Steuerwald & Montserrat Soler-López & Sandrine Curtet & Anne-Laure Vitte & Jérôme Govin & Jonathan Gaucher & Karin Sadoul & Darren J. Hart & Jeroen Krijgsv, 2009. "Cooperative binding of two acetylation marks on a histone tail by a single bromodomain," Nature, Nature, vol. 461(7264), pages 664-668, October.
    • Handle: RePEc:nat:nature:v:461:y:2009:i:7264:d:10.1038_nature08397
    DOI: 10.1038/nature08397
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    Cited by:

    1. Masaki Kikuchi & Satoshi Morita & Masatoshi Wakamori & Shin Sato & Tomomi Uchikubo-Kamo & Takehiro Suzuki & Naoshi Dohmae & Mikako Shirouzu & Takashi Umehara, 2023. "Epigenetic mechanisms to propagate histone acetylation by p300/CBP," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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