Efficient repression by a heterodimeric repressor in Escherichia coli.
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.
Webster
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ICI Joint Laboratory, University of Leicester, UK.
Merryweather
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Brammar
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D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics*; D008969:Molecular Sequence Data; D009875:Operator Regions, Genetic; D010957:Plasmids; D012097:Repressor Proteins / Q000378:metabolism*; D014764:Viral Proteins
C063367:434-repressor protein, Bacteriophage 434; D004269:DNA, Bacterial; D012097:Repressor Proteins; D014764:Viral Proteins