By Mark S. Mooseker
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Chem. 259, 14184-14189. Albanesi, J. , Hammer, J. , 111, Korn, E. , and Sheetz, M. P . (1985a). Monomeric Acanfhamoeba myosins I support movement of beads along actin cables. J . Eiol. Chem. 260, 8649-8652. Albanesi, J. , and Kom, E. (1985b). A kinetic model for the molecular basis of the contractile activity of Acanfhamoeba myosins IA and IB. J . Biol. Chem. 260, 11174-1 1179. Albanesi, J. ,and Korn, E. Effect of actin filament length and filament number concentration on the actin-activated ATPase activity of Acanrhamoeba myosin I.
Functional sequences on the myosin head. J . Muscle Res. Cell Motil. 10, 10-24. Pollard, T. , and Korn, E. D. (1973a). Acanrhamoeba myosin. 1. Isolation from Acanthamoeba castellanii of an enzyme similar to muscle myosin. J . Eiol. Chem. 248, 4682-4690. Pollard, T. , and Korn, E. D. (1973b). Acanthamoeba myosin. 11. Interaction with actin and with a new cofactor protein required for actin activation of Mg2+ -adenosine triphosphatase activity. J. Eiol. Chem. 248, 4691-4697. Pollard, T. , Weihing, R.
These results establish the existence of a regulatory cascade as shown in Fig. 5. VII. INTRACELLULAR LOCALIZATION In 1980, Gadasi and Korn found by immunofluorescence studies that the myosin I isozymes are located near the plasma membrane of Acanrhamoeba. This was confirmed in similar studies by Hagen et al. (1986). The earlier studies also showed that myosin I was associated with highly purified preparations of plasma membranes (Gadasi and Korn, 1980). These observations were extended by Miyata er al.