Enzymatic domain of human KIAA1718 for use in assays to identify drugs that modulate enzyme activity or to engineer hybrid enzymes for use in such assays.
- Acts as a promiscuous enzyme.
- Applications towards mental retardation, cleft lip or palate, and other congenital abnormalities.
Jumonji-C (JmjC) domain-containing proteins catalyze histone demethylation via an oxidative pathway that requires the presence of Fe(II) and α-ketoglutarate as cofactors. The active removal of methyl groups from histones plays an essential role in epigenetic regulation. These enzymes are involved in a range of cellular processes including DNA replication and repair as well as transcriptional activation and repression.
Emory researchers have isolated the catalytic jumonji domain of KIAA1718, a histone demethylase found in mice and humans that is selective for mono- and di-methylated lysine residues. The truncated protein behaves as a promiscuous enzyme, losing substrate specificity when the plant homeodomain (PHD) is deleted. Fusing the promiscuous jumonji domain and an epigenetic reader could generate hybrid enzymes to study histone posttranslational modifications.
Publications: Horton J, et al. Nature. 17:38-43. (2010).