Abstract
Regulation of the DNA binding affinity of an oligomeric protein can be considered to consist of an intrinsic component, in which the affinity of an individual DNA-binding domain is modulated in response to effector binding, and an extrinsic component, in which the relative position of the protein's two DNA-binding domains are altered so that they can or cannot contact both half-site operators simultaneously. We demonstrated directly that the TetR repressor utilizes an extrinsic mechanism and CAP, the catabolite activator protein, utilizes an intrinsic mechanism.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Allosteric Regulation
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Cyclic AMP / metabolism*
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Cyclic AMP Receptor Protein / chemistry
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Cyclic AMP Receptor Protein / metabolism*
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DNA / metabolism
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / metabolism
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Escherichia coli / chemistry
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Escherichia coli / metabolism*
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / metabolism*
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Protein Binding
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Repressor Proteins / chemistry
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Repressor Proteins / metabolism*
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Tetracycline / metabolism*
Substances
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Cyclic AMP Receptor Protein
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DNA-Binding Proteins
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Escherichia coli Proteins
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Repressor Proteins
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tetracycline resistance-encoding transposon repressor protein
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DNA
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Cyclic AMP
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Tetracycline