Our approaches include biochemical and structural studies of actin, myosin, and associated regulatory proteins. In addition, we have designed and developed in vitro assays for ATP-dependent movement of purified myosin on filaments reconstituted from purified actin. These assays allow us to analyze mutant myosin molecules for altered function. The site-directed mutagenized forms of myosin are obtained by gene cloning and expression in Dictyostelium. Our demonstration that the Dictyostelium myosin gene can undergo homologous recombination allows us to also probe the effects of the altered myosin forms on the phenotype of the cell.
Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin.
Myosin Structure and Function, Cold Spring Harbor Symposia on Quantitative Biology, Vol 60. Cold Spring Harbor Laboratory Press, pp. Cold-Sensitive Mutations of Dictyostelium. Myosin Heavy Chain Highlight Functional Domains of the Myosin Motor. Quantitative Measurements of Force and Displacement Using an Optical Trap.