Enzymatic activity and filament assembly of Acanthamoeba myosin II are regulated by adjacent domains at the end of the tail.
Polyclonal antibodies raised against a synthetic peptide consisting of the last 19 amino acids at the end of the coiled-coil region of the heavy chains inhibited the actin-activated Mg2+-ATPase activity of myosin II and its ability to form filaments. Antibodies against a synthetic peptide corresponding to the 21 adjacent amino acids at the beginning of the non-helical tailpiece, which include the three regulatory phosphorylatable serines, had no effect on either activity.
Atkinson
M A
MA
Laboratory of Cell Biology, National Heart, Lung and Blood Institute, Bethesda, MD 20892.
Appella
E
E
Corigliano-Murphy
M A
MA
Korn
E D
ED
D000048:Acanthamoeba / Q000201:enzymology*; D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D009218:Myosins / Q000378:metabolism*
D000199:Actins; D046911:Macromolecular Substances; D017301:Ca(2+) Mg(2+)-ATPase; D009218:Myosins