Abstract
We describe a new protein that binds to DNA and activates gene transcription in yeast. This protein, LexA-GAL4, is a hybrid of LexA, an Escherichia coli repressor protein, and GAL4, a Saccharomyces cerevisiae transcriptional activator. The hybrid protein, synthesized in yeast, activates transcription of a gene if and only if a lexA operator is present near the transcription start site. Thus, the DNA binding function of GAL4 can be replaced with that of a prokaryotic repressor without loss of the transcriptional activation function. These results suggest that DNA-bound LexA-GAL4 and DNA-bound GAL4 activate transcription by contacting other proteins.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacterial Proteins / genetics
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Bacterial Proteins / physiology*
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / physiology
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Fungal Proteins / genetics
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Fungal Proteins / physiology*
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Gene Expression Regulation*
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Operator Regions, Genetic
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Protein Binding
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Recombinant Proteins / genetics
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Recombinant Proteins / physiology*
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Repressor Proteins / physiology
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae / metabolism
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Serine Endopeptidases*
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Transcription, Genetic*
Substances
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Bacterial Proteins
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DNA-Binding Proteins
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Fungal Proteins
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LexA protein, Bacteria
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Recombinant Proteins
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Repressor Proteins
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Serine Endopeptidases