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Submitted on April 25, 2002
Accepted on August 12, 2002
1 Departments of Medicine, Biochemistry, Microbiology and Immunology, University of Ottawa, the Ottawa Health Research Institute, 725 Parkdale Ave, Ottawa, Ontario, Canada, K1Y 4E9
* To whom correspondence should be addressed. E-mail: qli{at}ohri.ca.
The effects of acetylation on gene expression are complex, with changes in chromatin accessibility intermingled with direct effects on transcriptional regulators. For the nuclear receptors, both positive and negative effects of acetylation on specific gene transcription have been observed. We report that p300 and SRC-1 interact transiently with the glucocorticoid receptor and that the acetyltransferase activity of p300 makes an important contribution to glucocorticoid receptor-mediated transcription. Treatment of cells with the deacetylase inhibitor sodium butyrate inhibited steroid-induced transcription and altered the transient association of GR with p300 and SRC-1. Additionally, sustained sodium butyrate treatment induced the degradation of p300 through the 26S proteasome pathway. Treatment with the proteasome inhibitor MG132 restored both the level of p300 protein and the transcriptional response to steroid over 20 h of treatment. These results reveal new levels for the regulatory control of gene expression by acetylation and suggest feedback control on p300 activity.
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