title: The yeast regulatory protein ADR1 binds in a zinc-dependent manner to the upstream activating sequence of ADH2.
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: D000426:Alcohol Dehydrogenase / Q000235:genetics*; D001483:Base Sequence; D004271:DNA, Fungal / Q000235:genetics; D004268:DNA-Binding Proteins / Q000502:physiology*; D005800:Genes, Fungal; D066298:In Vitro Techniques; D008667:Metalloproteins / Q000502:physiology*; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000235:genetics; D012045:Regulatory Sequences, Nucleic Acid; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D014157:Transcription Factors / Q000502:physiology*; D015032:Zinc / Q000502:physiology*
chemical_list: D004271:DNA, Fungal; D004268:DNA-Binding Proteins; D008667:Metalloproteins; D011993:Recombinant Fusion Proteins; D014157:Transcription Factors; D000426:Alcohol Dehydrogenase; D015032:Zinc