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Open Access Green as soon as Postprint is submitted to ZB.
The poly-serine domain of the lysyl-5 hydroxylase Jmjd6 mediates subnuclear localization.
Biochem. J. 453, 357-370 (2013)
Jmjd6 is an Fe(II) and 2-oxoglutarate (2OG) dependent oxygenase that catalyses hydroxylation of lysine residues in proteins involved in pre-mRNA splicing. Jmjd6 plays an essential role in vertebrate embryonic development and has been shown to modulate alternative splicing in response to hypoxic stress. Here we show that an alternatively spliced version of Jmjd6 lacking the polyS domain localises to the nucleolus, predominantly in the fibrillar centre. PolyS domain deleted Jmjd6 also interacts with nucleolar proteins. Furthermore, co-immunoprecipitation experiments and fluorescent 2-hybrid (F2H) assays demonstrate that Jmjd6 homo-oligomerisation occurs in cells. In correlation with the observed variations in the subnuclear distribution of Jmjd6 the structure of Jmjd6 oligomers in vitro changes in the absence of the polyS domain, possibly reflecting the role of the polyS domain in nuclear/nucleolar shuttling of Jmjd6.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Fe(ii)- And 2-oxoglutarate-dependent Oxygenase ; Jmjc ; Lysine Hydroxylation ; Nucleolus ; Polyserine Domain ; Pre-mrna Splicing; Hypoxia-inducible Factor ; Living Cells ; Phosphatidylserine Receptor ; Protein Interactions ; Mass-spectrometry ; Rna ; Visualization ; Nucleolus ; 2-oxoglutarate ; Identification
ISSN (print) / ISBN
0264-6021
e-ISSN
1470-8728
Journal
Biochemical Journal / Reviews
Quellenangaben
Volume: 453,
Issue: 3,
Pages: 357-370
Publisher
Portland Press
Non-patent literature
Publications
Reviewing status
Peer reviewed