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Jmjd6 (jumonji-domain-containing protein 6) is an Fe(II)- and 2OG (2-oxoglutarate)-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. In the present study we show that an alternatively spliced version of Jmjd6 lacking the polyS (polyserine) domain localizes to the nucleolus, predominantly in the fibrillar centre. Jmjd6 with the polyS domain deleted also interacts with nucleolar proteins. Furthermore, co-immunoprecipitation experiments and F2H (fluorescent 2-hybrid) assays demonstrate that Jmjd6 homo-oligomerization 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.

Original publication

DOI

10.1042/BJ20130529

Type

Journal article

Journal

Biochem J

Publication Date

01/08/2013

Volume

453

Pages

357 - 370

Keywords

Cell Line, Cell Nucleolus, Chromatography, Gel, Electrophoresis, Gel, Two-Dimensional, Fluorescence Recovery After Photobleaching, HeLa Cells, Humans, Immunoprecipitation, Jumonji Domain-Containing Histone Demethylases, Microscopy, Electron, Transmission, Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase, RNA Splicing