Εξειδίκευση τύπου :	Άρθρο σε επιστημονικό περιοδικό
Τίτλος:	Selective interactions of hnRNP M isoforms with the TET proteins TAF15 and TLS/FUS
Δημιουργός/Συγγραφέας:	Marko M. Leichter M. [EL] Πατρινού-Γεωργούλα, Μερόπη[EN] Patrinou-Georgoula, Meropi [EL] Γκιάλη, Αποστολία[EN] Guialis, Apostolia
Εκδότης:	Kluwer Academic Publishers
Ημερομηνία:	2014
Γλώσσα:	Αγγλικά
ISSN:	0301-4851
DOI:	10.1007/s11033-014-3128-3
Άλλο:	PubMed ID: 24474660
Περίληψη:	The molecular composition of macromolecular assemblies engaged in transcription and splicing influences biogenesis of mRNA transcripts. Preference for one over the other interactive protein partner within those complexes is expected to change the gene expression pattern and to affect subsequent cellular events. We report here the novel and selective associations between RNA-binding proteins, namely the hnRNP M1-4 isoforms - involved in early spliceosome assembly and alternative splicing - and the transcription factors TAF15 and TLS/FUS. In immunoprecipitation studies on HeLa nuclear extracts, TAF15 co-immunoprecipitates preferably with the higher molecular weight hnRNP M3/4 isoforms, opposite to TLS/FUS that associates with the lower molecular weight hnRNP M1/2 species. We demonstrate that these associations can be mediated through direct protein-protein interactions via the amino-termini of the TET proteins, independently of RNA. Finally, we show partial co-localization of TAF15 and TLS/FUS with hnRNP M proteins in HeLa nuclei, supporting the biochemically obtained data. The participation of hnRNP M in an expanding network of protein-protein interactions suggests its important functioning in the coordination of transcriptional and post-transcriptional events.
Τίτλος πηγής δημοσίευσης:	Molecular Biology Reports
Τόμος/Κεφάλαιο:	41
Τεύχος:	4
Σελίδες:	2687-2695
Θεματική Κατηγορία:	[EL] Βιολογία (Γενικά)[EN] Biology (General) [EL] Βιοχημεία[EN] Biochemistry
Λέξεις-Κλειδιά:	hnRNP M mRNA processing RNA-binding proteins TET proteins
Αξιολόγηση από ομότιμους (peer reviewed):	Ναι
Κάτοχος πνευματικών δικαιωμάτων:	© 2014 Springer Science+Business Media Dordrecht.
Σημειώσεις:	Sixth Framework Programme, FP6: MTKD-CT-2004-509836
Εμφανίζεται στις συλλογές:	Ινστιτούτο Χημικής Βιολογίας - Επιστημονικό έργο