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J. Biol. Chem., Vol. 277, Issue 41, 38095-38103, October 11, 2002
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From the Department of Biochemistry, University of Washington,
Seattle, Washington 98195-7350
The yeast transcriptional activator Adr1 controls
the expression of genes required for ethanol, glycerol, and fatty acid
utilization. We show that Adr1 acts directly on the promoters of
ADH2, ACS1, GUT1, CTA1,
and POT1 using chromatin immunoprecipitation assays. The
yeast homolog of the AMP-activated protein kinase, Snf1, promotes Adr1
chromatin binding in the absence of glucose, and the protein phosphatase complex, Glc7·Reg1, represses its binding in the
presence of glucose. A post-translational process is implicated in the regulation of Adr1 binding activity. Chromatin binding by Adr1 is not
the only step in ADH2 transcription that is regulated by glucose repression. Adr1 can bind to chromatin in repressed conditions in the presence of hyperacetylated histones. To study steps subsequent to promoter binding we utilized miniAdr1 transcription factors to
characterize Adr1-dependent transcription in
vitro. Yeast nuclear extracts prepared from glucose-repressed and
glucose-derepressed cells are equally capable of supporting
miniAdr1-dependent transcription and pre-initiation complex
formation. Nuclear extracts prepared from a snf1 mutant
support miniAdr1-dependent transcription but are partially
defective in the formation of pre-initiation complexes with Mediator
components being particularly depleted. We conclude that Snf1 regulates
Adr1-dependent transcription primarily at the level of
chromatin binding.
Snf1 Protein Kinase Regulates Adr1 Binding to Chromatin but Not
Transcription Activation*
,
*
This work was supported by Research Grant GM26079 from
NIGMS, National Institutes of Health (to E. T. Y.).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.
To whom correspondence should be addressed: Dept. of Biochemistry,
University of Washington, Box 357350, Seattle, WA 98195-7350. Tel.:
206-543-6517; Fax: 206-685-1792; E-mail: ety@u.washington.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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