Asymmetric allosteric activation of the symmetric ArgR hexamer

Research output: Contribution to journalArticle

Abstract

Hexameric arginine repressor, ArgR, bound to L-arginine serves both as the master transcriptional repressor/activator at diverse regulons in a wide range of bacteria and as a required cofactor for resolution of ColE1 plasmid multimers. Multifunctional ArgR is thus unusual in possessing features of specific gene regulators, global regulators, and non-specific gene organizers; its closest functional analog is probably CAP, the cyclic AMP receptor/activator protein. Isothermal titration calorimetry, surface plasmon resonance, and proteolysis indicate that binding of a single L-arginine residue per ArgR hexamer triggers a global conformational change and resets the affinities of the remaining five sites, making them 100-fold weaker. The analysis suggests a novel thermodynamic signature for this mechanism of activation. (C) 2004 Elsevier Ltd. All rights reserved.

Details

Authors
  • L H Jin
  • Wei-Feng Xue
  • J W Fukayama
  • J Yetter
  • M Pickering
  • J Carey
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Physical Chemistry
Original languageEnglish
Pages (from-to)43-56
JournalJournal of Molecular Biology
Volume346
Issue number1
Publication statusPublished - 2005
Publication categoryResearch
Peer-reviewedYes