抄録
Myosin is a molecular motor that drives movement of actin filaments. It was recently established that the myosin head undergoes a major shape change during the ATP hydrolysis cycle, leading to the popular hypothesis that the shape change provides motile force. Cellular slime mold is uniquely useful not only as an expression system of site-directed mutant myosins, but also as a genetic system to isolate specific mutant myosin genes and their suppressors out of a population of randomly mutagenized cells. Here we present the power of both sitedirected and random approaches to investigate the significance and mechanism of the conformational changes.
