UHRF1 recruits the histone acetyltransferase Tip60 and controls its expression and activity

作者:Achour Mayada; Fuhrmann Guy; Alhosin Mahmoud; Ronde Philippe; Chataigneau Thierry; Mousli Marc; Schini Kerth Valerie B; Bronner Christian*
来源:Biochemical and Biophysical Research Communications, 2009, 390(3): 523-528.
DOI:10.1016/j.bbrc.2009.09.131

摘要

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.

  • 出版日期2009-12-18