Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6

Research output: Contribution to journalJournal articleResearchpeer-review

  • M. Mantri
  • C.J. Webby
  • N.D. Loik
  • R.B. Hamed
  • M.A. McDonough
  • J.S.O. McCullagh
  • C.J. Schofield
  • A. Wolf
  • Nielsen, Michael Lund
  • A. Böttger
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. H-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. This journal is
Original languageEnglish
Issue number1
Pages (from-to)80-85
Number of pages6
Publication statusPublished - 1 Jan 2012

ID: 46455720