Fig. 1
From: An Msh3 ATPase domain mutation has no effect on MMR function
Electromobility shift assays. a Increasing concentrations of cold CA4 competitor induced substrate release by both Msh2-Msh3+/+ and Msh2-Msh3GD/GD heterodimers. Bars indicate that there is less than 10% difference between Msh2-Msh3GD/GD binding compared to wild type except at 20X molar ratio. b Increasing ATP concentration resulted in release of DNA binding in the Msh2-Msh3+/+ but not the Msh2-Msh3GD/GD nuclear extracts. Percent difference bars (set at 10%) show no overlap in binding upon addition of ATP