Journal
CHEMISTRY & BIOLOGY
Volume 11, Issue 3, Pages 295-299Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2004.03.001
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- NIGMS NIH HHS [GM-38627] Funding Source: Medline
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Treating yeast cells with rapamycin, a small molecule that inhibits the TOR proteins, leads to the repression of many genes [1, 2]. Consistent with prior studies, we find that RPD3, which encodes a histone deacetylase (HDAC), is required for repression upon rapamycin treatment. To elucidate the mechanism underlying RPD3-mediated repression, we screened all promoters in yeast for occupancy by Rpd3p before and after treatment with rapamycin. We find that Rpd3p binds to the promoters of rapamycin-repressible genes only following treatment. These data conflict with a previously proposed model suggesting that Rpd3p is constitutively bound to rapamycin-repressible genes and becomes active only after a stimulus such as treatment with rapamycin [3-5]. Rather, the comprehensive analysis presented here strongly supports a model in which recruitment of Rpd3p to gene promoters is a regulated step in the control of gene repression [6].
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