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Submitted on June 12, 2006
Accepted on January 8, 2007
Chromatin and Gene Expression Section, Laboratory of Molecular Carcinogenesis, National Institute of Environmental Health Sciences, National Institutes of Health, 111 Alexander Drive, P.O. Box 12233, Research Triangle Park, NC USA 27709
* To whom correspondence should be addressed. E-mail: archer1{at}niehs.nih.gov.
Histone acetylation is a highly dynamic post-translational modification that plays an important role in gene expression. Previous work showed that promoter histone deacetylation is accompanied by PR mediated activation of the mouse mammary tumor virus (MMTV) promoter. We investigated the role of this deacetylation and found that this histone deacetylation is not a singular event. In fact, histone acetylation at the MMTV promoter is highly dynamic, with an initial increase in acetylation followed by an eventual net deacetylation of histone H4. The timing of increase in acetylation of H4 coincides with the time at which PR, RNA polymerase II and histone acetyltransferases CBP and p300 are recruited to the MMTV promoter. The timing in which histone H4 deacetylation occurs (after PR and RNA polymerase II recruitment) and the limited effect trichostatin A and siRNA knockdown of HDAC 3 has on MMTV transcription suggests that this deacetylation activity is not required for the initiation of PR mediated transcription. Interestingly, HDAC1 and HDAC3, two histone deacetylases (HDACs) are already present at the MMTV prior to transcription activation. HDAC association at the MMTV promoter fluctuates during the hormone treatment. In particular, HDAC3 is temporarily undetected at the MMTV promoter within minutes after hormone treatment when the histone H4 acetylation increases but returns to the promoter near the time when histone acetylation levels start to decline. These results demonstrate the dynamic nature of coactivator/corepressor-promoter association and histone modifications such as acetylation during a transcription activation event.
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