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Asymmetric allosteric activation of the symmetric ArgR hexamer.

Jin, Lihua, Xue, Wei-Feng, Fukayama, June Wong, Yetter, Jaclyn, Pickering, Michael, Carey, Jannette (2005) Asymmetric allosteric activation of the symmetric ArgR hexamer. Journal of Molecular Biology, 346 (1). pp. 43-56. ISSN 0022-2836. (doi: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)

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. (Contact us about this Publication)
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
DOI/Identification number: 10.1016/j.jmb.2004.11.031
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 May 2019 10:17 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/34248 (The current URI for this page, for reference purposes)
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