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

Robert J. Klose, Kenichi Yamane, Yangjin Bae, Dianzheng Zhang, Hediye Erdjument-Bromage, Paul Tempst, Jiemin Wong and Yi Zhang ()
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Robert J. Klose: Howard Hughes Medical Institute
Kenichi Yamane: Howard Hughes Medical Institute
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

Nature, 2006, vol. 442, issue 7100, 312-316

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.

Date: 2006
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DOI: 10.1038/nature04853

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