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(Received for publication, December 3, 1996, and in revised form, February 25, 1997)
From the Adenine repression of the purine nucleotide
biosynthetic genes in Saccharomyces cerevisiae involves
down-regulation of the activator protein BAS1 or BAS2 by an unknown
mechanism. To determine the minimal cis-acting requirements for adenine
regulation, hybrid promoter constructs were made between
ADE5,7 promoter fragments and a CYC1-lacZ
reporter. A 139-nucleotide fragment containing two BAS1 binding sites
was sufficient to confer adenine regulation on the
CYC1-lacZ reporter. Analysis of deletion and substitution mutations led to the conclusion that the proximal BAS1 binding site is
both necessary and sufficient for regulation, whereas the distal site
augments the function of the proximal site. By performing saturation
mutagenesis, we found two essential regions that flank the proximal
site. An ABF1 consensus sequence is within one of these regions, and
mutations that impaired in vitro ABF1 binding impaired
promoter activity in vivo. A second region is AT-rich and
appears to bind BAS2. No substitution mutations led to high level
constitutive promoter activity as would be expected from removal of an
upstream repression sequence. Our results indicate that ABF1, BAS1, and
BAS2 are required for ADE5,7 promoter function and that
adenine repression most likely involves activator modification or a
negative regulator that does not itself bind DNA.
Volume 272, Number 20,
Issue of May 16, 1997
pp. 13343-13354
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
Department of Biology, Georgetown
University, Washington, D. C. 20057 and the ¶ Laboratory of
Eukaryotic Gene Regulation, NICHD, National Institutes of Health,
Bethesda, Maryland 20892
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