Cooperative tandem binding of met repressor of Escherichia coli

We present biochemical and genetic data to support the hypothesis that the Escherichia coli met repressor, MetJ, binds to synthetic and natural operator sequences in tandem arrays such that repression depends not only on the affinity of the DNA-protein interaction, but also on protein-protein contac...

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Bibliographic Details
Published inNature (London) Vol. 341; no. 6244; p. 711
Main Authors Phillips, S E, Manfield, I, Parsons, I, Davidson, B E, Rafferty, J B, Somers, W S, Margarita, D, Cohen, G N, Saint-Girons, I, Stockley, P G
Format Journal Article
LanguageEnglish
Published England 26.10.1989
Subjects
Apoproteins - biosynthesis
Apoproteins - metabolism
Bacterial Proteins - metabolism
Base Sequence
DNA, Bacterial - metabolism
Escherichia coli - metabolism
Escherichia coli Proteins
Genes, Bacterial
Models, Molecular
Molecular Sequence Data
Operator Regions, Genetic
Regulatory Sequences, Nucleic Acid
Repetitive Sequences, Nucleic Acid
Repressor Proteins - biosynthesis
Repressor Proteins - metabolism
Transcription Factors - metabolism
Tryptophan - metabolism
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Summary:We present biochemical and genetic data to support the hypothesis that the Escherichia coli met repressor, MetJ, binds to synthetic and natural operator sequences in tandem arrays such that repression depends not only on the affinity of the DNA-protein interaction, but also on protein-protein contacts along the tandem array. This represents a novel form of regulatory switch. Furthermore, there seems to be homology between the organization of the met and trp operators.
ISSN:0028-0836
1476-4687
DOI:10.1038/341711a0