Asymmetric allosteric activation of the symmetric ArgR hexamer.

Jin, Lihua and Xue, Wei-Feng and Fukayama, June Wong and Yetter, Jaclyn and Pickering, Michael and Carey, Jannette (2005) Asymmetric allosteric activation of the symmetric ArgR hexamer. Journal of Molecular Biology, 346 (1). pp. 43-56. ISSN 0022-2836. (doi:https://doi.org/10.1016/j.jmb.2004.11.031) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/doi:10.1016/j.jmb.2004.11.031

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-argine [corrected] per ArgR hexamer triggers a global conformation [corrected] 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.

Item Type: Article
Uncontrolled keywords: global analysis; cooperativity; c value; ligand occupancy
Subjects: Q Science > QC Physics
Q Science > QD Chemistry
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Wei-Feng Xue
Date Deposited: 11 Jun 2013 12:59 UTC
Last Modified: 29 Apr 2014 15:24 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/34248 (The current URI for this page, for reference purposes)
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