Jumonji domain containing protein 2A (JMJD2A) is an important reader and eraser of the histone code, responsible for specifically recognising trimethylated lysine 9 on histone H3 (H3K9me3) and catalysing its demethylation to H3K9me/H3K9me2. Since H3K9 is highly associated with regions of heterochromatin when methylated, and regions of euchromatin when acetylated, JMJD2A plays an important role in regulating the overall gene expression.
This tour around the crystallised structure of JMJD2A bound to H3K9me3 will show how JMJD2A recognises and binds H3K9me3, the function and binding of its necessary cofactors, and how the structure of JMJD2A forgoes some catalytic activity to ensure a high specificity for H3K9me3.
Original model generated from crystallography performed by Couture et al., 2007: doi:10.1038/nsmb1273
Figure 2 and 3 adapted from Klose, Kallin, & Zhang, 2006: https://doi.org/10.1038/nrg1945
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