Self-Hydroxylation of the splicing factor lysyl hydroxylase, JMJD6

Faculty of Pharmacy

Assiut University

Self-Hydroxylation of the splicing factor lysyl hydroxylase, JMJD6

Research Authors
Monica Mantri, Celia J. Webby, Nikita D. Loik, Refaat B. Hamed, Michael L. Nielsen, Michael A. McDonough, James S. O. McCullagha, Angelika Böttgerd, Christopher J. Schofield, Alexander Wolf
Research Department
Department of Pharmacognosy
Research Journal
MedChemComm
Research Rank
1
Research Vol
3
Research Year
2012
Research Member
Refaat Hamed
Research Abstract

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.