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

Jeanne Morinière, Sophie Rousseaux, Ulrich Steuerwald, Montserrat Soler-López, Sandrine Curtet, Anne-Laure Vitte, Jérôme Govin, Jonathan Gaucher, Karin Sadoul, Darren J. Hart, Jeroen Krijgsveld, Saadi Khochbin, Christoph W. Müller () and Carlo Petosa
Additional contact information
Jeanne Morinière: European Molecular Biology Laboratory, Grenoble Outstation, 6 rue Jules Horowitz, BP 181, 38042 Grenoble Cedex 9, France
Sophie Rousseaux: INSERM, U823
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
Sandrine Curtet: INSERM, U823
Anne-Laure Vitte: INSERM, U823
Jérôme Govin: INSERM, U823
Jonathan Gaucher: INSERM, U823
Karin Sadoul: INSERM, U823
Darren J. Hart: European Molecular Biology Laboratory, Grenoble Outstation, 6 rue Jules Horowitz, BP 181, 38042 Grenoble Cedex 9, France
Jeroen Krijgsveld: European Molecular Biology Laboratory, Meyerhofstrasse 1
Saadi Khochbin: INSERM, U823
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

Nature, 2009, vol. 461, issue 7264, 664-668

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.

Date: 2009
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DOI: 10.1038/nature08397

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