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J. Biol. Chem., Vol. 276, Issue 30, 28179-28184, July 27, 2001
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From the 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 human
immunodeficiency virus type 1 (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.
The Histone Acetyltransferase, hGCN5, Interacts with and
Acetylates the HIV Transactivator, Tat*
,
,
,
, and
Laboratoire de Biologie du Stress Oxydant,
Faculté de Pharmacie, Domaine de la Merci, 38700 La Tronche Cedex
and the § Laboratoire de Biologie Moléculaire et
Cellulaire de la Différenciation, INSERM U309, Institut Albert
Bonniot, Faculté de Médecine, Domaine de la Merci,
38706 La Tronche Cedex, France
*
This work was supported by Sidaction Contract
991249/23026-01-00/AO10-1 (to S. K.) and Contract
000013/30041-03-00/AO10-1 (to C. C.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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