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Papers In Press, published online ahead of print May 30, 2001
Institut Albert Bonniot, INSERM U309, La Tronche 38706
Corresponding Author: khochbin{at}ujf-grenoble.fr
Factor acetyltransferase activity associated with several histone acetyltransferases plays a key role in the control of transcription. Here we report that hGCN5, a well-known histone acetyltransferase, specifically interacts with and acetylates the HIV-1 transactivator protein, Tat. The interaction between Tat and hGCN5 is direct and involves the acetyltransferase and the bromodomain regions of hGCN5 as well as a limited region of Tat encompassing the cysteine-rich domain of the protein. Tat lysines 50 and 51, target of acetylation by p300/CBP, were also found to be acetylated by hGCN5. The acetylation of these two lysines by p300/CBP has been recently shown to stimulate Tat transcriptional activity and accordingly, we have found that hGCN5 can considerably enhance Tat-dependent transcription of the HIV-1 long terminal repeat. These data highlight the importance of the acetylation of lysines 50 and 51 in the function of Tat, since different histone acetyltransferases involved in distinct signaling pathways, GCN5 and p300/CBP, converge to acetylate Tat on the same site.
J. Biol. Chem, 10.1074/jbc.M101385200
Submitted on February 13, 2001
Revised on May 30, 2001
Accepted on May 30, 2001
The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat
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