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DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA

Author

Listed:
  • Steen K. T. Ooi

    (College of Physicians and Surgeons of Columbia University, New York, New York 10032, USA)

  • Chen Qiu

    (Emory University, Atlanta, Georgia 30322, USA)

  • Emily Bernstein

    (Laboratory of Chromatin Biology, The Rockefeller University, New York, New York 10021, USA)

  • Keqin Li

    (Emory University, Atlanta, Georgia 30322, USA)

  • Da Jia

    (Emory University, Atlanta, Georgia 30322, USA)

  • Zhe Yang

    (Emory University, Atlanta, Georgia 30322, USA)

  • Hediye Erdjument-Bromage

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

  • Paul Tempst

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

  • Shau-Ping Lin

    (Institute of Biotechnology, National Taiwan University, Taipei 106, Taiwan)

  • C. David Allis

    (Laboratory of Chromatin Biology, The Rockefeller University, New York, New York 10021, USA)

  • Xiaodong Cheng

    (Emory University, Atlanta, Georgia 30322, USA)

  • Timothy H. Bestor

    (College of Physicians and Surgeons of Columbia University, New York, New York 10032, USA)

Abstract

DNMT3L, a regulatory factor related in sequence to DNA methyltransferases, is shown to interact with the N terminus of histone H3 and this interaction is inhibited by methylation at lysine 4. This suggests DNMT3L could respond to states of histone modification to regulate de novo DNA methylation.

Suggested Citation

  • Steen K. T. Ooi & Chen Qiu & Emily Bernstein & Keqin Li & Da Jia & Zhe Yang & Hediye Erdjument-Bromage & Paul Tempst & Shau-Ping Lin & C. David Allis & Xiaodong Cheng & Timothy H. Bestor, 2007. "DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA," Nature, Nature, vol. 448(7154), pages 714-717, August.
    • Handle: RePEc:nat:nature:v:448:y:2007:i:7154:d:10.1038_nature05987
    DOI: 10.1038/nature05987
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