title: The fastest actin-based motor protein from the green algae, Chara, and its distinct mode of interaction with actin.
abstract: The endoplasmic streaming in Characean cells is an actin-dependent movement. The motor protein responsible for the streaming was partially purified and characterized. It was soluble at low ionic strength, an ATPase of a molecular mass of 225 kDa and activated more than 100 times by muscle F-actin. Surprisingly, in an in vitro motility assay, the motor protein moved muscle F-actin at 60 microns/s, which is similar to the velocity of streaming in a living cell and 10 times faster than muscle myosin. Proteolytic cleavage of actin impaired movement crucially on muscle myosin, but did not affect movement at all on the Chara motor protein, suggesting that the Chara motor protein would interact with actin via a set of sites different from those of muscle myosin.
mesh_terms: D000199:Actins / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D000460:Chlorophyta / Q000502:physiology*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D018482:Muscle, Skeletal / Q000502:physiology
chemical_list: D000199:Actins; D010450:Endopeptidases; D000251:Adenosine Triphosphatases