ACE1 transcription factor produced in Escherichia coli binds multiple regions within yeast metallothionein upstream activation sequences.
The ACE1 protein of Saccharomyces cerevisiae was expressed as a trpE-ACE1 fusion protein in Escherichia coli and shown to bind CUP1 upstream activation sequences at multiple regions in a copper-inducible manner. These binding sites contain within them the sequence 5'-TC(T)4-6GCTG-3', which we propose constitutes an important part of the ACE1 consensus recognition sequence.
Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor 48109-0606.
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Evans
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Engelke
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Thiele
D001483:Base Sequence; D001665:Binding Sites; D003300:Copper / Q000494:pharmacology; D004926:Escherichia coli; D005786:Gene Expression Regulation; D008668:Metallothionein / Q000235:genetics*; D008969:Molecular Sequence Data; D011401:Promoter Regions, Genetic; D011993:Recombinant Fusion Proteins; D012045:Regulatory Sequences, Nucleic Acid; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D014157:Transcription Factors / Q000502:physiology*; D014158:Transcription, Genetic
D011993:Recombinant Fusion Proteins; D014157:Transcription Factors; D003300:Copper; D008668:Metallothionein