2. Academic Validation
  3. Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing

Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing

  • Science. 2009 Jul 3;325(5936):90-3. doi: 10.1126/science.1175865.
Celia J Webby 1,  Alexander Wolf,  Natalia Gromak,  Mathias Dreger,  Holger Kramer,  Benedikt Kessler,  Michael L Nielsen,  Corinna Schmitz,  Danica S Butler,  John R Yates 3rd,  Claire M Delahunty,  Phillip Hahn,  Andreas Lengeling,  Matthias Mann,  Nicholas J Proudfoot,  Christopher J Schofield,  Angelika Böttger
Affiliations

Affiliation

  • 1 Chemistry Research Laboratory and Oxford Centre for Integrative Systems Biology, University of Oxford, 12 Mansfield Road, Oxford, Oxon OX1 3TA, UK.
PMID: 19574390 DOI: 10.1126/science.1175865
Abstract

The finding that the metazoan hypoxic response is regulated by oxygen-dependent posttranslational hydroxylations, which regulate the activity and lifetime of hypoxia-inducible factor (HIF), has raised the question of whether other hydroxylases are involved in the regulation of gene expression. We reveal that the splicing factor U2 small nuclear ribonucleoprotein auxiliary factor 65-kilodalton subunit (U2AF65) undergoes posttranslational lysyl-5-hydroxylation catalyzed by the Fe(II) and 2-oxoglutarate-dependent dioxygenase Jumonji domain-6 protein (Jmjd6). Jmjd6 is a nuclear protein that has an important role in vertebrate development and is a human homolog of the HIF asparaginyl-hydroxylase. Jmjd6 is shown to change alternative RNA splicing of some, but not all, of the endogenous and reporter genes, supporting a specific role for Jmjd6 in the regulation of RNA splicing.

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