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EMBO reports 5, 5, 490–496 (2004)
doi:10.1038/sj.embor.7400139
Published online: 23 April 2004
Tethering of HP1 proteins to chromatin is relieved by phosphoacetylation of histone H3
Bogdan Mateescu1, Patrick England2, Frederic Halgand3, Moshe Yaniv1 & Christian Muchardt1
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1 Expression Génétique et Maladies, URA1644 du CNRS, Département de Biologie du Développement, Institut Pasteur, Bât. Fernbach, 25, Rue du Docteur Roux, 7S724, Paris Cedex 15, France
2 Plate-Forme de Biophysique des Protéines et de leurs Interactions, Département de Biologie Structurale et Chimie, Institut Pasteur, 28 Rue du Docteur Roux, 7S724, Paris Cedex 15, France
3 Laboratoire de Spectrométrie de Masse, Institut de Chimie des Substances Naturelles, CNRS, 1 Avenue de la Terrasse, 91198 Gif-sur-Yvette, France
To whom correspondence should be addressed
Christian Muchardt Tel: +33 1 45 68 85 13/+33 1 45 68 85 25; Fax: +33 1 40 61 30 33; E-mail: muchardt@pasteur.fr
Received 29 September 2003; Accepted 2 March 2004; Published online 23 April 2004.
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Abstract
Histone H3 lysine 9 methylation is associated with long-term transcriptional repression through recruitment of heterochromatin protein 1 (HP1) proteins. These proteins are believed to promote the formation of dense chromatin structures interfering with DNA accessibility. During the G2 phase of the cell cycle, HP1 proteins are delocalized from foci of pericentromeric heterochromatin, while a wave of H3 serine 10 phosphorylation is initiated within these regions. Here, we show that in vivo phosphorylation of serine 10 in G2 can occur on histone tails methylated on lysine 9. Unexpectedly, this modification favours rather than prevents HP1 binding to chromatin. Dissociation of HP1 from the methylated histone H3 tails is observed only after a third modification by acetylation of lysine 14, which occurs in prophase. We propose that phosphoacetylation of histone H3 could be a general mechanism allowing the cell to overcome HP1-mediated transcriptional repression.
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