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The Fe(II) and 2-oxoglutarate dependent oxygenase Jmjd6 has been shown to hydroxylate lysine residues in the essential splice factor U2 auxiliary factor 65 kDa subunit (U2AF65) and to act as a modulator of alternative splicing. We describe further evidence for the role of Jmjd6 in the regulation of pre-mRNA processing including interactions of Jmjd6 with multiple arginine-serine-rich (RS)-domains of SR- and SR-related proteins including U2AF65, Luc7-like protein 3 (Luc7L3), SRSF11 and Acinus S', but not with the bona fide RS-domain of SRSF1. The identified Jmjd6 target proteins are involved in different mRNA processing steps and play roles in exon dependent alternative splicing and exon definition. Moreover, we show that Jmjd6 modifies splicing of a constitutive splice reporter, binds RNA derived from the reporter plasmid and punctually co-localises with nascent RNA. We propose that Jmjd6 exerts its splice modulatory function by interacting with specific SR-related proteins during splicing in a RNA dependent manner.

Original publication

DOI

10.1093/nar/gku488

Type

Journal article

Journal

Nucleic Acids Res

Publication Date

07/2014

Volume

42

Pages

7833 - 7850

Keywords

Alternative Splicing, HEK293 Cells, HeLa Cells, Humans, Jumonji Domain-Containing Histone Demethylases, Nuclear Proteins, Protein Interaction Domains and Motifs, RNA, RNA, Messenger, RNA-Binding Proteins, Ribonucleoproteins, Serine-Arginine Splicing Factors, Splicing Factor U2AF