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EMBO reports 4, 6, 575–580 (2003)
doi:10.1038/sj.embor.embor861
Published online: 30 May 2003
MYC recruits the TIP60 histone acetyltransferase complex to chromatin
Scott R. Frank1, Tiziana Parisi1, Stefan Taubert1, Paula Fernandez1, 4, Miriam Fuchs2, Ho-Man Chan2, David M. Livingston2 & Bruno Amati1, 3
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1 DNAX Research Institute, 901 California Avenue, Palo Alto, California 94304, USA
2 Dana–Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA
3 Department of Experimental Oncology, European Institute of Oncology, Via Ripamonti 435, 20141 Milan, Italy
4 Present address: University of Bern, Länggass-Strasse 122, CH-3001 Bern, Switzerland
To whom correspondence should be addressed
Bruno Amati Tel: +39 02 57 489 824; Fax: +39 02 57 489 851; bruno.amati@ieo-research.org
Received 24 October 2002; Accepted 16 April 2003; Published online 30 May 2003.
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Abstract
The transcription factor MYC binds specific DNA sites in cellular chromatin and induces the acetylation of histones H3 and H4. However, the histone acetyltransferases (HATs) that are responsible for these modifications have not yet been identified. MYC associates with TRRAP, a subunit of distinct macromolecular complexes that contain the HATs GCN5/PCAF or TIP60. Although the association of MYC with GCN5 has been shown, its interaction with TIP60 has never been analysed. Here, we show that MYC associates with TIP60 and recruits it to chromatin in vivo with four other components of the TIP60 complex: TRRAP, p400, TIP48 and TIP49. Overexpression of enzymatically inactive TIP60 delays the MYC-induced acetylation of histone H4, and also reduces the level of MYC binding to chromatin. Thus, the TIP60 HAT complex is recruited to MYC-target genes and, probably with other other HATs, contributes to histone acetylation in response to mitogenic signals.
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