Issue 1, 2012

Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6

Abstract

The lysyl5S-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.

Graphical abstract: Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6

Supplementary files

Article information

Article type
Concise Article
Submitted
01 Sep 2011
Accepted
19 Oct 2011
First published
18 Nov 2011

Med. Chem. Commun., 2012,3, 80-85

Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6

M. Mantri, C. J. Webby, N. D. Loik, R. B. Hamed, M. L. Nielsen, M. A. McDonough, J. S. O. McCullagh, A. Böttger, C. J. Schofield and A. Wolf, Med. Chem. Commun., 2012, 3, 80 DOI: 10.1039/C1MD00225B

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