The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3

Paul A. C. Cloos, Jesper Christensen, Karl Agger, Alessio Maiolica, Juri Rappsilber, Torben Antal, Klaus H. Hansen and Kristian Helin ()
Additional contact information
Paul A. C. Cloos: Biotech Research & Innovation Centre
Jesper Christensen: Biotech Research & Innovation Centre
Karl Agger: Biotech Research & Innovation Centre
Alessio Maiolica: FIRC Institute of Molecular Oncology
Juri Rappsilber: FIRC Institute of Molecular Oncology
Torben Antal: Biotech Research & Innovation Centre
Klaus H. Hansen: Biotech Research & Innovation Centre
Kristian Helin: Biotech Research & Innovation Centre

Nature, 2006, vol. 442, issue 7100, 307-311

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/nature04837

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