The yeast regulatory protein ADR1 binds in a zinc-dependent manner to the upstream activating sequence of ADH2.
Open Access
- 1 October 1988
- journal article
- research article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 8 (10) , 4552-4556
- https://doi.org/10.1128/mcb.8.10.4552
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.This publication has 32 references indexed in Scilit:
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