Abstract
We have determined the kinetic and motile properties of a myosin 5a HMM construct in which four calmodulin-binding IQ motifs are replaced by the putative single alpha helical domain (SAH) of similar length from Dictyostelium myosin, MyoM. Electron microscopy of this chimera showed that the SAH domain was straight and 17 nm long as predicted, restoring the truncated lever to the length of wild type (Myo5-6IQ). The powerstroke (21.5 nm) measured in the optical trap was slightly less than that for Myo5-6IQ (25 nm) but much greater than for Myo5-2IQ (10 nm).
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