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Post-translational modifications of histones H3 and H4 associated with the histone methyltransferases Suv39h1 and G9a

Philippe Robin1, Lauriane Fritsch1, Ophélie Philipot1, Fedor Svinarchuk2 and Slimane Ait-Si-Ali1*

Author Affiliations

1 Centre National de la Recherche Scientifique (CNRS) FRE 2944, Institut André Lwoff, rue Guy Moquet, Villejuif F-94801, France; Université Paris-Sud, Villejuif F-94801, France

2 Centre National de la Recherche Scientifique (CNRS) FRE 3018, GENETHON, bis rue de l'Internationale, Evry F-91002, France; Université d'Evry, Evry F-91002, France

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Genome Biology 2007, 8:R270  doi:10.1186/gb-2007-8-12-r270

Published: 20 December 2007

Abstract

Specific combinations of post-translational modifications of histones alter chromatin structure, facilitating gene transcription or silencing. Here we have investigated the 'histone code' associated with the histone methyltransferases Suv39h1 and G9a by combining double immunopurification and mass spectrometry. Our results confirm the previously reported histone modifications associated with Suv39h1 and G9a. Moreover, this method allowed us to demonstrate for the first time an association of acetylated histones with the repressor proteins Suv39h1 and G9a.