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

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 () and Timothy H. Bestor ()
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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

Nature, 2007, vol. 448, issue 7154, 714-717

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.

Date: 2007
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DOI: 10.1038/nature05987

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