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The yeast regulatory protein ADR1 binds in a zinc-dependent manner to the upstream activating sequence of ADH2
A Eisen1, W E Taylor, H Blumberg
1Department of Biochemistry, University of Washington, Seattle 98195.
Molecular and Cellular Biology
|October 1, 1988
Abstract:
The yeast ADR1 protein contains two zinc finger domains that are essential for its role in transcriptional activation of alcohol dehydrogenase (ADH2). These domains are thought to function as DNA-binding structures. An ADR1-beta-galactosidase fusion protein made in Escherichia coli and containing the finger domains of ADR1 binds in vitro in a zinc-dependent manner to DNA fragments containing the two ADH2 upstream activation sequences. The strongest binding is to upstream activation sequence 1, a 22-base-pair palindrome.