| Literature DB >> 3141794 |
A Eisen1, W E Taylor, H Blumberg, E T Young.
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.Entities:
Mesh:
Substances:
Year: 1988 PMID: 3141794 PMCID: PMC365534 DOI: 10.1128/mcb.8.10.4552-4556.1988
Source DB: PubMed Journal: Mol Cell Biol ISSN: 0270-7306 Impact factor: 4.272