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J. Biol. Chem., Vol. 275, Issue 21, 16160-16166, May 26, 2000
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From the The Zap1 transcriptional activator of
Saccharomyces cerevisiae plays a major role in zinc
homeostasis by inducing the expression of several genes under
zinc-limited growth conditions. This activation of gene expression is
mediated by binding of the protein to one or more zinc-responsive
elements present in the promoters of its target genes. To better
understand how Zap1 functions, we mapped its DNA binding domain using a
combined in vivo and in vitro approach. Our
results show that the Zap1 DNA binding domain maps to the carboxyl-terminal 194 amino acids of the protein; this region contains
five of its seven potential zinc finger domains. Fusing this region to
the Gal4 activation domain complemented a zap1
Mapping the DNA Binding Domain of the Zap1 Zinc-responsive
Transcriptional Activator*
,,,¶
Department of Nutritional Sciences,
University of Missouri, Columbia, Missouri 65211 and the
§ Departments of Hematology and Biochemistry, University of
Utah Health Sciences Center, Salt Lake City, Utah 84132
mutation
for low zinc growth and also conferred high level expression on a
zinc-responsive element-lacZ reporter. In
vitro, the purified 194-residue fragment bound to DNA with a high
affinity (dissociation constant in the low nanomolar range) similar to
that of longer fragments of Zap1. Furthermore, by deletion and
site-directed mutagenesis, we demonstrated that each of the five
carboxyl-terminal zinc fingers are required for high affinity DNA binding.
*
This work was supported by National Institutes of Health
Grant GM58265.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.
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