Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases.

By J. Whetstine, A. Nottke, F. Lan, Maite Huarte, S. Smolikov, Zhongzhou Chen, E. Spooner, E. Li, Gongyi Zhang, M. Colaiácovo and 1 more. Cell, 2006

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Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact (2012, positive): “The KDM2 and KDM3 families were unable to demethylate trimethylated lysines; however, this lack of activity was remedied by the discovery of the first tri-demethylase family, KDM4A-KDM4D (also known as JMJD2A-JMJD2D) (Figure 1A) (Cloos et al., 2006; Fodor et al., 2006; Klose et al., 2006; Trojer et ”
JmjC-domain-containing proteins and histone demethylation (2006, background): “D) methylation 15–18 .”
The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36 (2006, background): “Duringtherevisionofourmanuscript,anotherstudyreported that JHDM3A is a me3-speciﬁc H3K9/H3K36 demethylase, with little activity towards lower modiﬁcation states 23 .”
The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases. (2007, positive): “We used a candidate approach ( Whetstine et al., 2006 ) to search for H3K4me3 histone demethylases, focusing on approximately 28 human JmjC-domain-containing”