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• W2076454996 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." @default.
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• W2076454996 date "2005-02-01" @default.
• W2076454996 modified "2023-10-03" @default.
• W2076454996 title "Asymmetric Allosteric Activation of the Symmetric ArgR Hexamer" @default.
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• W2076454996 doi "https://doi.org/10.1016/j.jmb.2004.11.031" @default.
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