z-logo
open-access-imgOpen Access
DNA Binding Activity of theEscherichia coliNitric Oxide Sensor NorR Suggests a Conserved Target Sequence in Diverse Proteobacteria
Author(s) -
Nicholas P. Tucker,
Benoît D’Autréaux,
David J. Studholme,
Stephen Spiro,
Ray Dixon
Publication year - 2004
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.186.19.6656-6660.2004
Subject(s) - biology , escherichia coli , genetics , dna , enterobacteriaceae , conserved sequence , proteobacteria , sequence (biology) , base sequence , biochemistry , microbiology and biotechnology , bacteria , gene , 16s ribosomal rna
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here