MyoD-E12 heterodimers and MyoD-MyoD homodimers are equally stable

Biochemistry
S J MalekiB K Hurlburt

Abstract

Muscle development is controlled by the MyoD family of basic helix-loop-helix (bHLH) DNA-binding proteins. These proteins dimerize with ubiquitous products of the E2A gene (E12 and E47) and bind in a sequence-specific manner to enhancer regions of muscle-specific genes activating their expression. In this study, fluorescence anisotropy has been utilized to characterize the interactions of recombinant MyoD and E12 in solution in the absence of DNA. The Gibb's free energies of dissociation (deltaG) and the equilibrium dissociation constants (K(D)) for the protein-protein interactions are reported. The deltaG for the MyoD homodimers in 100 mM KCl was 8.7 kcal/mol (K(D) = 340 nM), and increasing the salt concentration resulted in destabilization of the dimer. From titrations of MyoD-dansyl with E12 at 100 mM KCl, a free energy of heterodimerization of 8.7 (+0.4/-2.4) kcal/mol was recovered using rigorous confidence limit testing. The titrations of E12-dansyl with MyoD yielded a free energy of 8.3 kcal/mol with tighter confidence limits, +0.5/-0.8 kcal/mol. Thus, in the absence of DNA, both MyoD homodimers and MyoD-E12 heterodimers are relatively weak complexes of approximately the same stability. E12 does not form stable homo-oligo...Continue Reading

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Citations

Dec 14, 2004·Chembiochem : a European Journal of Chemical Biology·Amy C BeltranJoel M Gottesfeld
Apr 26, 2013·Open Biology·Qiang ZhangMelvin E Andersen
Oct 3, 2007·Proteins·Daniel P RyanJacqueline M Matthews
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Jun 20, 2019·Development Genes and Evolution·Damian LewandowskiMałgorzata Daczewska

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