Physarum myosin light chain interacts with actin in a Ca2+-dependent manner.
Actin-modulating activity was analysed with the 16,131-dalton calcium-binding light chain (CaLc, Kobayashi et al. (1988) J. Biol. Chem. 263, 305-313) of Physarum myosin, which is under an inhibitory Ca-control (Kohama and Kendrick-Jones (1986) J. Biochem. 99, 1433-1446). When skeletal muscle actin was polymerized in the presence of CaLc and Ca2+, increases in both viscosity and birefringence were reduced under high shear conditions. However, CaLc did not inhibit actin polymerization under no or low shearing forces, which was demonstrated by a variety of methods including fluorescence intensity measurements using pyrenyl actin. We propose that actin polymerized in the presence of CaLc and Ca2+ is easily fragmented under high shearing forces to produce the changes in viscosity and birefringence.
Kohama
K
K
Department of Pharmacology, Faculty of Medicine, University of Tokyo.
Oosawa
M
M
Ito
T
T
Maruyama
K
K
D000199:Actins / Q000378:metabolism* / Q000648:ultrastructure; D001718:Birefringence; D002118:Calcium / Q000378:metabolism*; D008854:Microscopy, Electron; D009218:Myosins / Q000378:metabolism*; D010804:Physarum / Q000378:metabolism*; D011108:Polymers; D014783:Viscosity
D000199:Actins; D011108:Polymers; D009218:Myosins; D002118:Calcium