PuSH - Publikationsserver des Helmholtz Zentrums München

Heim, A.* ; Grimm, C.* ; Müller, U.* ; Häußler, S.* ; Mackeen, M.M.* ; Merl, J. ; Hauck, S.M. ; Kessler, B.M.* ; Schofield, C.J.* ; Wolf, A. ; Böttger, A.*

Jumonji domain containing protein 6 (Jmjd6) modulates splicing and specifically interacts with arginine-serine-rich (RS) domains of SR- and SR-like proteins.

Nucleic Acids Res. 42, 7833-7850 (2014)
Verlagsversion Volltext DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
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.
Altmetric
Weitere Metriken?
[➜Einloggen]
Zusatzinfos bearbeiten [➜Einloggen]
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Hypoxia-inducible Factor; Vegf-receptor 1; Phosphatidylserine Receptor; Apoptotic Cells; Proteomic Analysis; Lysyl Hydroxylase; Mammalian-cells; Label-free; Rna; Recognition
ISSN (print) / ISBN 0305-1048
e-ISSN 1362-4962
Zeitschrift Nucleic Acids Research
Quellenangaben Band: 42, Heft: 12, Seiten: 7833-7850 Artikelnummer: , Supplement: ,
Verlag Oxford University Press
Verlagsort Oxford
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) CF Metabolomics & Proteomics (CF-MPC)
Institute of Molecular Toxicology and Pharmacology (TOXI)