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J. Biol. Chem., Vol. 277, Issue 17, 15171-15181, April 26, 2002
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From the Post-translational modifications of histones play
an important role in modulating gene transcription within chromatin. We used the mouse mammary tumor virus (MMTV) promoter, which adopts an
ordered nucleosomal structure, to investigate the impact of a specific
inhibitor of histone deacetylase, trichostatin A (TSA), on
progesterone receptor-activated transcription. TSA induced global histone hyperacetylation, and this effect occurred independently of the presence of hormone. Interestingly, chromatin
immunoprecipitation analysis revealed no significant change in the
level of acetylated histones associated with the MMTV promoter
following high TSA treatment. In human breast cancer cells, in which
the MMTV promoter adopts a constitutively "open" chromatin
structure, treatment with TSA converted the MMTV promoter into a closed
structure. Addition of hormone did not overcome this TSA-induced
closure of the promoter chromatin. Furthermore, TSA treatment resulted in the eviction of the transcription factor nuclear factor-1 from the
promoter and reduced progesterone receptor-induced transcription. Kinetic experiments revealed that a loss of chromatin-remodeling proteins was coincident with the decrease in MMTV transcriptional activity and the imposition of repressed chromatin architecture at the
promoter. These results demonstrate that deacetylase inhibitor treatment at levels that induce global histone acetylation may leave
specific regulatory regions relatively unaffected and that this
treatment may lead to transcriptional inhibition by mechanisms that
modify chromatin-remodeling proteins rather than by influencing histone
acetylation of the local promoter chromatin structure.
The Histone Deacetylase Inhibitor Trichostatin A Blocks
Progesterone Receptor-mediated Transactivation of the Mouse Mammary
Tumor Virus Promoter in Vivo*
,, and¶
Laboratory of Reproductive and Developmental
Toxicology, NIEHS, National Institutes of Health, Research Triangle
Park, North Carolina 27709 and the § Departments of
Obstetrics and Gynaecology and Biochemistry, University of Western
Ontario, London, Ontario N6A 4L6, Canada
*
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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