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J. Biol. Chem., Vol. 277, Issue 51, 49459-49465, December 20, 2002
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From the Department of Biochemistry and Molecular Biology, Colorado
State University, Fort Collins, Colorado 80523-1870
The human T-cell leukemia virus (HTLV-I)-encoded
Tax protein is a potent transcriptional activator that stimulates
expression of the integrated provirus. Biochemical studies indicate
that Tax, together with cellular transcription factors, interacts with viral cAMP-response element enhancer elements to recruit the
pleiotropic coactivators CREB-binding protein and p300. Histone
acetylation by these coactivators has been shown to play a major role
in activating HTLV-I transcription from chromatin templates in
vitro. However, the extent of histone modification and the
precise identity of the cellular regulatory proteins bound at the
HTLV-I promoter in vivo is not known. Chromatin
immunoprecipitation analysis was used to investigate factor binding and
histone modification at the integrated HTLV-I provirus in infected
T-cells (SLB-1). These studies reveal the presence of Tax, a variety of
ATF/CREB and AP-1 family members (CREB, CREB-2, ATF-1, ATF-2,
c-Fos, and c-Jun), and both p300 and CREB-binding protein at the
HTLV-I promoter. Consistent with the binding of these coactivators, we
observed histone H3 and H4 acetylation at three regions within the
proviral genome. Histone deacetylases were also present at the viral
promoter and, following their inhibition, we observe an increase in
histone H4 acetylation on the HTLV-I promoter and a concomitant
increase in viral RNA. Together, these results suggest that a variety
of transcriptional activators, coactivators, and histone deacetylases participate in the regulation of HTLV-I transcription in infected T-cells.
Transcription Factor Binding and Histone Modifications on the
Integrated Proviral Promoter in Human T-cell Leukemia
Virus-I-infected T-cells*
,,
*
This study was supported by NCI, National Institutes of
Health, Grants CA-55035 (to J. K. N.) and CA-87540 (to J. K. N. and P. J. L.).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.
Both authors contributed equally to this work.
§
To whom correspondence should be addressed. Tel.: 970-491-0420;
E-mail: jnyborg@lamar.colostate.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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