Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases

• DOI: 10.1038/ncomms11974
• Publication Date: 2016-06-23T20:19:36Z
• Authors: Louise J. Walport; Richard J. Hopkinson; Rasheduzzaman Cho...; Rachel Schiller; Wei Ge; Akane Kawamura; Christopher J. Sc...
• Keywords: Demethylation; RDM

Abstract While the oxygen-dependent reversal of lysine N ɛ -methylation is well established, existence bona fide ω -methylarginine demethylases (RDMs) controversial. Lysine demethylation, as catalysed by two families (the flavin-dependent KDM1 enzymes and 2-oxoglutarate- JmjC KDMs, respectively), proceeds via oxidation -methyl group, resulting in release formaldehyde. Here we report detailed biochemical studies clearly demonstrating that, purified form, a subset KDMs can also act RDMs, both on histone non-histone fragments, formaldehyde release. RDM catalysis studied using peptides wild-type sequences known to be arginine-methylated which KDM’s methylated target substituted for arginine. Notably, preferred sequence requirements KDM activity vary even with same enzymes. The demonstration isolated will stimulate efforts detect biologically relevant activity.