Reversible superprecipitation and bundle formation of plasmodium actomyosin.
Synthetic actomyosin from plasmodium was found to undergo reversible superprecipitation upon addition of ATP. According to electronmicroscopic investigation upon clearing, short myosin filaments of about 0.2 micron in length appeared predominantly coexisting with actin filaments, and after superprecipitation, bundles of actin filaments were formed where short myosin filaments or myosin molecules were bound to the side of the bundle, making a whisk-like structure. The turbidity and the ATPase activity of actomyosin were measured at various ATP concentrations clamped by using an ATP-regenerating system. The turbidity was high below 1 . 10(-6) M ATP, corresponding to the state of superprecipitation, and with increasing ATP concentration it dropped in the range of 1 . 10(-6)--1 . 10(-5) M ATP. On the other hand, the ATPase activity was low below 1 . 10(-6) M ATP and increased above 1 . 10(-5) M after the turbidity dropped. Characteristic features of superprecipitation of plasmodium actomyosin observed here were discussed in relation to the mechanism of motility in vivo.
D000199:Actins / Q000378:metabolism; D000205:Actomyosin / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate; D007700:Kinetics; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D009218:Myosins / Q000378:metabolism; D009235:Myxomycetes / Q000378:metabolism*; D010804:Physarum / Q000378:metabolism*; D011487:Protein Conformation
D000199:Actins; D046911:Macromolecular Substances; D000255:Adenosine Triphosphate; D000205:Actomyosin; D000251:Adenosine Triphosphatases; D009218:Myosins