Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6
Mantri M., Webby CJ., Loik ND., Hamed RB., Nielsen ML., McDonough MA., McCullagh JSO., Böttger A., Schofield CJ., Wolf A.
The lysyl 5S-hydroxylase, JMJD6 acts on proteins involved in RNA splicing. We find that in the absence of substrate JMJD6 catalyses turnover of 2OG to succinate. 1H-NMR analyses demonstrate that consumption of 2OG is coupled to succinate formation. MS analyses reveal that JMJD6 undergoes self-hydroxylation in the presence of Fe(ii) and 2OG resulting in production of 5S-hydroxylysine residues. JMJD6 in human cells is also found to be hydroxylated. Self-hydroxylation of JMJD6 may play a regulatory role in modulating the hydroxylation status of proteins involved in RNA splicing. © The Royal Society of Chemistry.