DNA binding activity of the Escherichia coli nitric oxide sensor NorR suggests a conserved target sequence in diverse proteobacteria.
The Escherichia coli nitric oxide sensor NorR was shown to bind to the promoter region of the norVW transcription unit, forming at least two distinct complexes detectable by gel retardation. Three binding sites for NorR and two integration host factor binding sites were identified in the norR-norV intergenic region. The derived consensus sequence for NorR binding sites was used to search for novel members of the E. coli NorR regulon and to show that NorR binding sites are partially conserved in other members of the proteobacteria.
Tucker
Nicholas P
NP
John Innes Centre, Colney, Norwich, United Kingdom.
D'Autréaux
Benoît
B
Studholme
David J
DJ
Spiro
Stephen
S
Dixon
Ray
R
D000595:Amino Acid Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D004247:DNA / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D009569:Nitric Oxide / Q000378:metabolism*; D020560:Proteobacteria / Q000737:chemistry*; D015534:Trans-Activators / Q000378:metabolism*
D029968:Escherichia coli Proteins; D015534:Trans-Activators; D009569:Nitric Oxide; D004247:DNA