Jmjd6 Catalyses Lysyl-Hydroxylation of U2AF65, a Protein Associated with RNA Splicing-Reference-Cited by-同舟云学术

Jmjd6 Catalyses Lysyl-Hydroxylation of U2AF65, a Protein Associated with RNA Splicing

Published:2009-07-03 Issue:5936 Volume:325 Page:90-93
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Webby Celia J.¹,Wolf Alexander²,Gromak Natalia³,Dreger Mathias⁴,Kramer Holger⁵,Kessler Benedikt⁵,Nielsen Michael L.⁶,Schmitz Corinna²,Butler Danica S.¹,Yates John R.⁷,Delahunty Claire M.⁷,Hahn Phillip⁸,Lengeling Andreas⁸⁹,Mann Matthias⁶,Proudfoot Nicholas J.³,Schofield Christopher J.¹,Böttger Angelika²

Affiliation:

1. Chemistry Research Laboratory and Oxford Centre for Integrative Systems Biology, University of Oxford, 12 Mansfield Road, Oxford, Oxon OX1 3TA, UK.

2. Department of Biology II, Ludwig-Maximilians-University, Munich, Großhaderner Strasse 2, D-82152 Planegg-Martinsried, Germany.

3. Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, Oxon OX1 3RE, UK.

4. Department of Physiology, Anatomy, and Genetics, University of Oxford, Parks Road, Oxford, Oxon OX1 3PT, UK.

5. Henry Wellcome Building for Molecular Physiology, University of Oxford, Oxford, OX3 7BN, UK.

6. Department of Proteomics and Signal Transduction, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.

7. Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA 92037, USA.

8. Research Group Infection Genetics, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.

9. Roslin Institute and Royal (Dick) School of Veterinary Studies, University of Edinburgh, EBVC, Roslin, EH25 9RG, UK.

Abstract

Modifying the Modifier 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. (p. 90 ) 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 mini-gene.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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