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Issue 1, 2012
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Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6

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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.

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

  • This article is part of the themed collection: Epigenetics
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Publication details

The article was received on 01 Sep 2011, accepted on 19 Oct 2011 and first published on 18 Nov 2011


Article type: Concise Article
DOI: 10.1039/C1MD00225B
Citation: Med. Chem. Commun., 2012,3, 80-85
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    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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