title: Regulation of the actin-activated ATPase activity of Acanthamoeba myosin II by copolymerization with phosphorylated and dephosphorylated peptides derived from the carboxyl-terminal end of the heavy chain.
abstract: Myosin II from Acanthamoeba castellanii is a conventional myosin composed of two heavy chains and two pairs of light chains. The amino-terminal approximately 90 kDa of each heavy chain form a globular head that contains the ATPase site and an ATP-sensitive actin-binding site. The carboxyl-terminal approximately 80 kDa of both heavy chains interact to form a coiled coil, helical rod (through which the molecules self-associate into bipolar filaments) ending in a short nonhelical tailpiece. Phosphorylation of 3 serine residues at the tip of the tail (at positions 11, 16, and 21 from the carboxyl terminus) inactivates the actin-activated Mg2(+)-ATPase activity of myosin II filaments. Previous work had indicated that the activity of each myosin II molecule in a filament reflects the global state of phosphorylation of the filament rather than the phosphorylation state of the molecule itself. We have now purified the approximately 28-kDa carboxyl-terminal region of the heavy chain lacking the last two phosphorylation sites, and we have shown that this peptide copolymerizes with and regulates the actin-activated Mg2(+)-ATPase activities of native dephosphorylated and phosphorylated myosin II. It can be concluded from these studies that the biologically relevant enzymatic activity of myosin II is regulated by a phosphorylation-dependent conformational change in the myosin filaments.
authors: Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.
authors: C
authors: C
authors: Ganguly
authors: M A
authors: MA
authors: Atkinson
authors: A K
authors: AK
authors: Attri
authors: V
authors: V
authors: Sathyamoorthy
authors: B
authors: B
authors: Bowers
authors: E D
authors: ED
authors: Korn
mesh_terms: D000048:Acanthamoeba / Q000201:enzymology*; D000199:Actins / Q000378:metabolism*; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D007700:Kinetics; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008961:Models, Structural; D008970:Molecular Weight; D015879:Myosin Subfragments / Q000302:isolation & purification / Q000378:metabolism; D009218:Myosins / Q000378:metabolism* / Q000648:ultrastructure; D010766:Phosphorylation
chemical_list: D000199:Actins; D046911:Macromolecular Substances; D015879:Myosin Subfragments; D017301:Ca(2+) Mg(2+)-ATPase; D009218:Myosins