UHRF1 recruits the histone acetyltransferase Tip60 and controls its expression and activity |
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Authors: | Mayada Achour Mahmoud Alhosin Thierry Chataigneau Valérie B Schini-Kerth |
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Institution: | a CNRS UMR 7213, Université de Strasbourg, Faculté de Pharmacie, 74 route du Rhin, 67401 Illkirch, France b EA4438 Physiopathologie et Médecine translationnelle, Faculté de Médecine, Université de Strasbourg, 3 rue Koeberlé, 67000 Strasbourg, France |
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Abstract: | Tat-interactive protein, 60 kDa (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. |
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Keywords: | DNMT1 DNA methyltransferase 1 H2AK5 lysine 5 of histone H2A HDAC1 histone deacetylase 1 Tip60 Tat-interactive protein of 60 kDa UHRF1 Ubiquitin-like PHD Ringer Finger 1 |
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