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SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation

Author

Listed:
  • Alejandro Vaquero

    (Howard Hughes Medical Institute, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School
    Present address: ICREA and IBMB-CSIC/IRB, Parc Cientific de Barcelona, Josep Samitier 1–5, 08028 Barcelona, Spain.)

  • Michael Scher

    (Howard Hughes Medical Institute, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School
    NYU-Medical School, 522 First Avenue, New York, New York 10016, USA)

  • Hediye Erdjument-Bromage

    (Molecular Biology Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, New York 10021, USA)

  • Paul Tempst

    (Molecular Biology Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, New York 10021, USA)

  • Lourdes Serrano

    (Human Genetics Institute, Rutgers University, 145 Bevier Road, Piscataway, New Jersey 08854, USA)

  • Danny Reinberg

    (Howard Hughes Medical Institute, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School
    NYU-Medical School, 522 First Avenue, New York, New York 10016, USA)

Abstract

SUV39H1 is the major methyltransferase responsible for tri-methylation of histone H3 at lysine 9 in heterochromatin. The histone deacetylase SIRT1 is shown to target the SUV39H1 enzyme and contribute to elevated levels of SUV39H1 activity and H3K9me3 in heterochromatin.

Suggested Citation

  • Alejandro Vaquero & Michael Scher & Hediye Erdjument-Bromage & Paul Tempst & Lourdes Serrano & Danny Reinberg, 2007. "SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation," Nature, Nature, vol. 450(7168), pages 440-444, November.
    • Handle: RePEc:nat:nature:v:450:y:2007:i:7168:d:10.1038_nature06268
    DOI: 10.1038/nature06268
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