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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Asymmetric allosteric activation of the symmetric ArgR hexamer.

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.[1]

References

  1. Asymmetric allosteric activation of the symmetric ArgR hexamer. Jin, L., Xue, W.F., Fukayama, J.W., Yetter, J., Pickering, M., Carey, J. J. Mol. Biol. (2005) [Pubmed]
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