Quantitative analysis of DNA binding by the Escherichia coli arginine repressor

Danuta Szwajkajzer, Lizhong Dai, June Wong Fukayama, Bozena Abramczyk, Robert Fairman, Jannette Carey

Research output: Contribution to journalArticle

25 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)949-962
Number of pages14
JournalJournal of Molecular Biology
Volume312
Issue number5
DOIs
StatePublished - Oct 5 2001

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Keywords

  • Analytical ultracentrifugation
  • Bending
  • Recombination
  • Transcription
  • Trimer

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