@article{3270,
  keywords = {Repressor Proteins, Escherichia coli, Base Sequence, Bacterial Proteins, Nucleic Acid Conformation, Substrate Specificity, DNA, Bacterial, Protein Binding, Escherichia coli Proteins, DNA-Binding Proteins, Thermodynamics, Protein Subunits, Protein Structure, Quaternary, Allosteric Regulation, Allosteric Site, Apoproteins, Ultracentrifugation},
  author = {D Szwajkajzer and L Dai and J Fukayama and B Abramczyk and R Fairman and J Carey},
  title = {Quantitative analysis of DNA binding by the Escherichia coli arginine repressor.},
  abstract = { <p>Allosteric activation of the hexameric arginine repressor (ArgR) for specific operator DNA binding appears to involve alteration in its quaternary structure. Current models for activation include subunit assembly and/or domain rearrangements in response to binding of the coeffector l-arginine. To investigate the molecular basis for ArgR operator interactions, we have carried out a series of quantitative analyses of ArgR subunit assembly and of the affinity, stoichiometry, cooperativity, and l-arginine- and DNA sequence-dependence of ArgR-DNA binding. The results indicate that subunit assembly plays no role in activation, although communication among subunits of the ArgR hexamer is required for specific DNA binding. The data suggest that DNA is also an allosteric effector of ArgR.</p> },
  year = {2001},
  journal = {J Mol Biol},
  volume = {312},
  pages = {949-62},
  month = {2001 Oct 05},
  issn = {0022-2836},
  doi = {10.1006/jmbi.2001.4941},
  language = {eng},
}