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The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36

Author

Listed:
  • Robert J. Klose

    (Howard Hughes Medical Institute
    Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill)

  • Kenichi Yamane

    (Howard Hughes Medical Institute
    Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill)

  • Yangjin Bae

    (Baylor College of Medicine)

  • Dianzheng Zhang

    (Baylor College of Medicine)

  • Hediye Erdjument-Bromage

    (Molecular Biology Program, Memorial Sloan Kettering Cancer Center)

  • Paul Tempst

    (Molecular Biology Program, Memorial Sloan Kettering Cancer Center)

  • Jiemin Wong

    (Baylor College of Medicine)

  • Yi Zhang

    (Howard Hughes Medical Institute
    Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill)

Abstract

Up to the mark Two papers in this issue identify enzymes capable of demethylating a trimethyl group from the Lys 9 residue of histone H3 — a 'mark' required for the establishment of heterochromatin and previously considered stable. Cloos et al. show that GASC1, a member of the JMJD2 enzyme family, can disrupt heterochromatin structure when overexpressed and may contribute to tumour development. Klose et al. show that overexpression of JHDM3A, also a JMJD2-type enzyme, disrupts heterochromatin structure. It may function in euchromatin to regulate transcription.

Suggested Citation

  • Robert J. Klose & Kenichi Yamane & Yangjin Bae & Dianzheng Zhang & Hediye Erdjument-Bromage & Paul Tempst & Jiemin Wong & Yi Zhang, 2006. "The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36," Nature, Nature, vol. 442(7100), pages 312-316, July.
    • Handle: RePEc:nat:nature:v:442:y:2006:i:7100:d:10.1038_nature04853
    DOI: 10.1038/nature04853
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