UHRF1 recruits the histone acetyltransferase Tip60 and controls its expression and activity.
Fiche publication
Date publication
décembre 2009
Auteurs
Membres identifiés du Cancéropôle Est :
Dr BRONNER Christian, Dr RONDE Philippe, Pr SCHINI-KERTH Valérie, Dr FUHRMANN Guy, Dr MOUSLI Marc
Tous les auteurs :
Achour M, Fuhrmann G, Alhosin M, Ronde P, Chataigneau T, Mousli M, Schini-Kerth VB, Bronner C
Lien Pubmed
Résumé
Tat-interactive protein, 60kDa (Tip60) is a histone acetyltransferase with specificity toward lysine 5 of histone H2A (H2AK5) and plays multiple roles in chromatin remodeling processes. Co-immunoprecipitation experiments performed on Jurkat cells, showed that Tip60 is present in the same macro-molecular complex as UHRF1 (Ubiquitin-like containing PHD and RING domain 1), DNMT1 (DNA methyltransferase 1), and HDAC1 (histone deacetylase 1). Furthermore, immunocytochemistry experiments confirmed that Tip60 co-localizes with the UHRF1/DNMT1 complex. Although down-regulation of UHRF1 by RNA interference enhanced Tip60 expression, a significant decrease of the level of acetylated H2AK5 was observed. Consistently, we have observed that down-regulation of Tip60 and DNMT1 by RNA interference, dramatically reduced the levels of acetylated H2AK5. Altogether, these results suggest that Tip60 is a novel partner of the epigenetic integration platform interplayed by UHRF1, DNMT1 and HDAC1 involved in the epigenetic code replication.
Référence
Biochem Biophys Res Commun. 2009 Dec 18;390(3):523-8