作者: Kenichi Yamane , Charalambos Toumazou , Yu-ichi Tsukada , Hediye Erdjument-Bromage , Paul Tempst
DOI: 10.1016/J.CELL.2006.03.027
关键词:
摘要: Summary Covalent modification of histones plays an important role in regulating chromatin dynamics and transcription. Histone methylation was thought to be irreversible until recently. Using a biochemical assay coupled with chromatography, we have purified JmjC domain-containing protein, JHDM2A, which specifically demethylates mono- dimethyl-H3K9. Similar JHDM1, JHDM2A-mediated histone demethylation requires cofactors Fe(II) α-ketoglutarate. Mutational studies indicate that domain zinc finger present JHDM2A are required for its enzymatic activity. Overexpression greatly reduced the H3K9 level vivo. Knockdown results increase dimethyl-K9 levels at promoter region subset genes concomitant decrease their expression. Finally, exhibits hormone-dependent recruitment androgen-receptor target genes, resulting transcriptional activation. Thus, our work identifies demethylase links function