Substitutions at auxiliary operator O3 enhance repression by nitrate-responsive regulator NarL at synthetic lac control regions in Escherichia coli K-12.
We constructed monocopy lac operon control regions in which the operators O1-lac and O3-lac were replaced by NarL and NarP binding sites from the nirB or napF operon control regions. The results support the hypothesis that DNA-bound dimers of phospho-NarL can participate in higher-order cooperative interactions.
Stewart
Valley
V
Section of Microbiology, University of California, One Shields Avenue, Davis CA 95616-8665, USA. vjstewart@ucdavis.edu
Bledsoe
Peggy J
PJ
D001483:Base Sequence; D001665:Binding Sites; D003433:Crosses, Genetic; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D019281:Dimerization; D048168:Escherichia coli K12 / Q000235:genetics / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000235:genetics* / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D007700:Kinetics; D007763:Lac Operon / Q000235:genetics*; D008969:Molecular Sequence Data; D016254:Mutagenesis, Insertional; D010766:Phosphorylation; D001616:beta-Galactosidase / Q000235:genetics
D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C069780:NarL protein, E coli; D001616:beta-Galactosidase