Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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.

Original publication




Journal article



Publication Date





90 - 93


Alternative Splicing, Amino Acid Sequence, Biocatalysis, Cell Line, Chromatography, Liquid, HeLa Cells, Humans, Hydroxylation, Jumonji Domain-Containing Histone Demethylases, Lysine, Molecular Sequence Data, Nuclear Proteins, Protein Processing, Post-Translational, RNA, Small Interfering, Receptors, Cell Surface, Recombinant Proteins, Ribonucleoproteins, Splicing Factor U2AF, Tandem Mass Spectrometry, Tropomyosin