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Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription
Journal article

Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription

  • Di Cerbo, Vincenzo Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany
  • Mohn, Fabio Institute of Molecular Biotechnology, Vienna, Austria
  • Ryan, Daniel P Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee, United Kingdom
  • Montellier, Emilie Faculté de Médecine, Institut Albert Bonniot, Grenoble, France
  • Kacem, Salim Institut de Génétique Moléculaire, CNRS UMR5535/Université de Montpellier I and II, Montpellier, France
  • Tropberger, Philipp Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany
  • Kallis, Eleni Institute for Biophysics, Ulm University, Ulm, Germany
  • Holzner, Monika Institute for Biophysics, Ulm University, Ulm, Germany
  • Hoerner, Leslie Friedrich Miescher Institute for Biomedical Research (FMI), Basel, Switzerland
  • Feldmann, Angelika Friedrich Miescher Institute for Biomedical Research (FMI), Basel, Switzerland
  • Richter, Florian Martin Cellular Immunobiology, Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany
  • Bannister, Andrew J Department of Pathology, University of Cambridge, Cambridge, United Kingdom
  • Mittler, Gerhard Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany
  • Michaelis, Jens Institute for Biophysics, Ulm University, Ulm, Germany
  • Khochbin, Saadi Faculté de Médecine, Institut Albert Bonniot, Grenoble, France
  • Feil, Robert Institut de Génétique Moléculaire, CNRS UMR5535/Université de Montpellier I and II, Montpellier, France
  • Schuebeler, Dirk Friedrich Miescher Institute for Biomedical Research (FMI), Basel, Switzerland
  • Owen-Hughes, Tom Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee, United Kingdom
  • Daujat, Sylvain Department of Functional Genomics, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS UMR, Strasbourg, France
  • Schneider, Robert Department of Functional Genomics, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS UMR, Strasbourg, France
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  • 2014-3-25
Published in:
  • eLife. - eLife Sciences Publications, Ltd. - 2014, vol. 3
English Post-translational modifications of proteins have emerged as a major mechanism for regulating gene expression. However, our understanding of how histone modifications directly affect chromatin function remains limited. In this study, we investigate acetylation of histone H3 at lysine 64 (H3K64ac), a previously uncharacterized acetylation on the lateral surface of the histone octamer. We show that H3K64ac regulates nucleosome stability and facilitates nucleosome eviction and hence gene expression in vivo. In line with this, we demonstrate that H3K64ac is enriched in vivo at the transcriptional start sites of active genes and it defines transcriptionally active chromatin. Moreover, we find that the p300 co-activator acetylates H3K64, and consistent with a transcriptional activation function, H3K64ac opposes its repressive counterpart H3K64me3. Our findings reveal an important role for a histone modification within the nucleosome core as a regulator of chromatin function and they demonstrate that lateral surface modifications can define functionally opposing chromatin states.
Language
  • English
Open access status
gold
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Persistent URL
https://sonar.ch/global/documents/56665
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