Modifying the Modifier

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Science Signaling  07 Jul 2009:
Vol. 2, Issue 78, pp. ec227
DOI: 10.1126/scisignal.278ec227

Covalent modification of proteins provides an important means whereby their function is regulated. Hydroxylation, catalyzed by oxygenase enzymes, plays an important role in the response to hypoxia, for example. The human protein Jmjd6 has been thought to act as an oxygenase, catalyzing the demethylation of histone H3 at arginine-2 and histone H4 at arginine-3. Webby et al. now show that Jmjd6 interacts with the messenger RNA splicing factor U2AF65 and acts to hydroxylate this protein at lysine residues, modifications also seen in vivo. Furthermore, Jmjd6 modulates the alternative splicing of both an endogenous gene and an introduced minigene.

C. J. Webby, A. Wolf, N. Gromak, M. Dreger, H. Kramer, B. Kessler, M. L. Nielsen, C. Schmitz, D. S. Butler, J. R. Yates III, C. M. Delahunty, P. Hahn, A. Lengeling, M. Mann, N. J. Proudfoot, C. J. Schofield, A. Böttger, Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing. Science 325, 90–93 (2009). [Abstract] [Full Text]

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