title: Enzymatic activity and filament assembly of Acanthamoeba myosin II are regulated by adjacent domains at the end of the tail.
abstract: 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.
authors.affiliation: Laboratory of Cell Biology, National Heart, Lung and Blood Institute, Bethesda, MD 20892.
authors.forename: M A
authors.initials: MA
authors.lastname: Atkinson
authors.forename: E
authors.initials: E
authors.lastname: Appella
authors.forename: M A
authors.initials: MA
authors.lastname: Corigliano-Murphy
authors.forename: E D
authors.initials: ED
authors.lastname: Korn
mesh_terms: 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*
chemical_list: D000199:Actins; D046911:Macromolecular Substances; D017301:Ca(2+) Mg(2+)-ATPase; D009218:Myosins