Characterization of kinesin switch I mutations that cause hereditary spastic paraplegia
Fig 2
MT affinity in the presence of AMPPNP.
MT pelleting assays were performed as described for Fig 1, except 5 mM AMPPNP was substituted in the reaction buffer. Experiments were repeated in a range of tubulin concentrations from 0 to 20 μM and the results of the densitometry analysis of the western blots produced are plotted for each Kif5A mutant. The curves shown are the best fit to the data using the exponential decay function in Origin 8 in a user free computational method. A) Curves of fraction Kif5A bound as a function of tubulin concentration for the wild type and mutant proteins. B-H) Individual Kif5A curves (WT or mutant as indicated) with mean +/- SD for each concentration of tubulin analyzed.