Efficient repression by a heterodimeric repressor in Escherichia coli.

C Webster; A Merryweather; W Brammar

doi:10.1111/j.1365-2958.1992.tb01480.x

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Efficient repression by a heterodimeric repressor in Escherichia coli.

C Webster·A Merryweather·W Brammar

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Abstract

Previous studies with purified variants of the 434 repressor having different operator-binding specificities have demonstrated the interactions of a heterodimeric repressor with a hybrid operator site. The present study investigates the interactions between the 434 repressor and its operator site. The optimum 434 operator half-site is used with a P22 operator half-site to create a hybrid 434/P22 operator. We show that this hybrid operator can be efficiently bound by a heterodimeric repressor, consisting of one wild-type 434 repressor monomer and one 434 repressor monomer with the binding specificity of the P22 repressor, to bring about repression in Escherichia coli.

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Amino Acid Sequence Cloning, Molecular DNA, Bacterial Escherichia coli Molecular Sequence Data Operator Regions, Genetic Plasmids Repressor Proteins Viral Proteins Journal Article Research Support, Non-U.S. Gov't

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C Webster, A Merryweather, W Brammar. 1992. Efficient repression by a heterodimeric repressor in Escherichia coli.. https://doi.org/10.1111/j.1365-2958.1992.tb01480.x

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