Coordinated methyl and RNA binding is required for heterochromatin localization of mammalian HP1<i>α</i>

  • Christian Muchardt
    Expression Génétique et Maladies, Biologie du Développement, Institut Pasteur 25 rue du Dr‐Roux F‐75724 Paris cedex 15 France
  • Marie Guillemé
    Expression Génétique et Maladies, URA1644 du CNRS, Institut Pasteur Paris
  • Jacob‐S Seeler
    Unité de Recombinaison et Expression Génétique, Institut National de la Santé et da la Recherche Médicale U163, Institut Pasteur Paris
  • Didier Trouche
    Laboratoire de Biologie Moléculaire Eucaryote, UMR 5099 CNRS, and Ligue Nationale Contre le Cancer, Institut de Biologie Cellulaire et Génétique Toulouse France
  • Anne Dejean
    Unité de Recombinaison et Expression Génétique, Institut National de la Santé et da la Recherche Médicale U163, Institut Pasteur Paris
  • Moshe Yaniv
    Expression Génétique et Maladies, URA1644 du CNRS, Institut Pasteur Paris

抄録

<jats:p>In mammalian cells, as in <jats:italic>Schizosaccharomyces pombe</jats:italic> and <jats:italic>Drosophila</jats:italic>, HP1 proteins bind histone H3 tails methylated on lysine 9 (K9). However, whereas K9‐methylated H3 histones are distributed throughout the nucleus, HP1 proteins are enriched in pericentromeric heterochromatin. This observation suggests that the methyl‐binding property of HP1 may not be sufficient for its heterochromatin targeting. We show that the association of HP1α with pericentromeric heterochromatin depends not only on its methyl‐binding chromo domain but also on an RNA‐binding activity present in the hinge region of the protein that connects the conserved chromo and chromoshadow domains. Our data suggest the existence of complex heterochromatin binding sites composed of methylated histone H3 tails and RNA, with each being recognized by a separate domain of HP1α.</jats:p>

収録刊行物

  • EMBO reports

    EMBO reports 3 (10), 975-981, 2002-10

    Springer Science and Business Media LLC

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