2.50
Hdl Handle:
http://hdl.handle.net/10033/78493
Title:
Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing.
Authors:
Webby, Celia J; Wolf, Alexander; Gromak, Natalia; Dreger, Mathias; Kramer, Holger; Kessler, Benedikt; Nielsen, Michael L; Schmitz, Corinna; Butler, Danica S; Yates, John R; Delahunty, Claire M; Hahn, Phillip; Lengeling, Andreas; Mann, Matthias; Proudfoot, Nicholas J; Schofield, Christopher J; Böttger, Angelika
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.
Affiliation:
Chemistry Research Laboratory and Oxford Centre for Integrative Systems Biology, University of Oxford, 12 Mansfield Road, Oxford, Oxon OX1 3TA, UK.
Citation:
Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing. 2009, 325 (5936):90-3 Science
Journal:
Science (New York, N.Y.)
Issue Date:
3-Jul-2009
URI:
http://hdl.handle.net/10033/78493
DOI:
10.1126/science.1175865
PubMed ID:
19574390
Type:
Article
Language:
en
ISSN:
1095-9203
Appears in Collections:
publications of the department infection genetics (INFG)

Full metadata record

DC FieldValue Language
dc.contributor.authorWebby, Celia J-
dc.contributor.authorWolf, Alexander-
dc.contributor.authorGromak, Natalia-
dc.contributor.authorDreger, Mathias-
dc.contributor.authorKramer, Holger-
dc.contributor.authorKessler, Benedikt-
dc.contributor.authorNielsen, Michael L-
dc.contributor.authorSchmitz, Corinna-
dc.contributor.authorButler, Danica S-
dc.contributor.authorYates, John R-
dc.contributor.authorDelahunty, Claire M-
dc.contributor.authorHahn, Phillip-
dc.contributor.authorLengeling, Andreas-
dc.contributor.authorMann, Matthias-
dc.contributor.authorProudfoot, Nicholas J-
dc.contributor.authorSchofield, Christopher J-
dc.contributor.authorBöttger, Angelika-
dc.date.accessioned2009-08-25T13:11:27Z-
dc.date.available2009-08-25T13:11:27Z-
dc.date.issued2009-07-03-
dc.identifier.citationJmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing. 2009, 325 (5936):90-3 Scienceen
dc.identifier.issn1095-9203-
dc.identifier.pmid19574390-
dc.identifier.doi10.1126/science.1175865-
dc.identifier.urihttp://hdl.handle.net/10033/78493-
dc.description.abstractThe 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.en
dc.language.isoenen
dc.subject.meshAlternative Splicingen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshBiocatalysisen
dc.subject.meshCell Lineen
dc.subject.meshChromatography, Liquiden
dc.subject.meshHela Cellsen
dc.subject.meshHumansen
dc.subject.meshHydroxylationen
dc.subject.meshLysineen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshNuclear Proteinsen
dc.subject.meshProtein Processing, Post-Translationalen
dc.subject.meshRNA, Small Interferingen
dc.subject.meshReceptors, Cell Surfaceen
dc.subject.meshRecombinant Proteinsen
dc.subject.meshRibonucleoproteinsen
dc.subject.meshTandem Mass Spectrometryen
dc.subject.meshTropomyosinen
dc.titleJmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing.en
dc.typeArticleen
dc.contributor.departmentChemistry Research Laboratory and Oxford Centre for Integrative Systems Biology, University of Oxford, 12 Mansfield Road, Oxford, Oxon OX1 3TA, UK.en
dc.identifier.journalScience (New York, N.Y.)en

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