1974•Proceedings of the National Academy of SciencesOpen access

Interaction of the Operator of the Tryptophan Operon with Repressor

John K. Rose, Charles Yanofsky

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Abstract

Transcription studies in vitro on repression of the tryptophan operon of Escherichia coli show that partially purified trp repressor binds specifically to DNA containing the trp operator with a repressor-operator dissociation constant of about 0.2 nM in 0.12 M salt at 37 degrees , a value consistent with the extent of trp operon regulation in vivo. The half-life of the trp repressor-trp operator complex is less than 2 min in vitro in 0.12 M salt.

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Transcription studies in vitro on repression of the tryptophan operon of Escherichia coli show that partially purified trp repressor binds specifically to DNA containing the trp operator with a repressor-operator dissociation constant of about 0.2 nM in 0.12 M salt at 37 degrees , a value consistent with the extent of trp operon regulation in vivo. The half-life of the trp repressor-trp operator complex is less than 2 min in vitro in 0.12 M salt.

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Available abstract

Transcription studies in vitro on repression of the tryptophan operon of Escherichia coli show that partially purified trp repressor binds specifically to DNA containing the trp operator with a repressor-operator dissociation constant of about 0.2 nM in 0.12 M salt at 37 degrees , a value consistent with the extent of trp operon regulation in vivo. The half-life of the trp repressor-trp operator complex is less than 2 min in vitro in 0.12 M salt.

Key concepts: trp operon, Operon, Repressor, Tryptophan, Operator (biology), gal operon, Transcription (linguistics), L-arabinose operon

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