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PMID: 3141794 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The yeast regulatory protein ADR1 binds in a zinc-dependent manner to the upstream activating sequence of ADH2.

Molecular and cellular biology ·Vol. 8 ·No. 10 ·1988-10-00 ·Pages 4552-6

Eisen A, Taylor WE, Blumberg H, Young ET

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.

MeSH Terms
Alcohol Dehydrogenase/genetics Base Sequence DNA, Fungal/genetics DNA-Binding Proteins/physiology Genes, Fungal In Vitro Techniques Metalloproteins/physiology Molecular Sequence Data Recombinant Fusion Proteins/genetics Regulatory Sequences, Nucleic Acid Saccharomyces cerevisiae/genetics Transcription Factors/physiology Zinc/physiology
Chemicals
DNA, Fungal DNA-Binding Proteins Metalloproteins Recombinant Fusion Proteins Transcription Factors Alcohol Dehydrogenase Zinc
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Eisen A
Department of Biochemistry, University of Washington, Seattle 98195.
Taylor W E
Blumberg H
Young E T
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27 references, click to expand
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/mcb.8.10.4552-4556.1988
Published
1988-10-00
Pages
4552-6
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC365534
Subset
IM
Grants
NIGMS NIH HHS · GM-26079 · United States
Databases
GENBANK
M23389
External Links
PubMed source DOI: 10.1128/mcb.8.10.4552-4556.1988 PMC Full Text View journal details
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