Zigzag motions of the myosin-coated beads actively sliding along actin filaments suspended between immobilized beads.

The motions of myosin filaments actively sliding along suspended actin filaments were studied. By manipulating a double-beam laser tweezers, single actin filaments were suspended between immobilized microbeads. When another beads coated with myosin filaments were dragged to suspended actin filaments, the beads instantly and unidirectionally slid along the actin filaments. The video image analysis showed that the beads slid at a velocity of ca. 3-5 microm/s accompanied with zigzag motions. When beads were densely coated with myosin filaments, the sliding motions became straight and smooth. The obtained results indicate that (1) during the sliding motions, the interaction between myosin heads and actin filaments is weak and susceptible to random thermal agitations, (2) the effects of thermal agitations to the sliding motions of myofilaments are readily suppressed by mechanical constraints imposed to the filaments, and (3) the active sliding force is produced almost in parallel to the filaments axis.

[1]  T. Yanagida,et al.  Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap. , 1994, Biophysical journal.

[2]  K Matsuno,et al.  ATP-dependent fluctuations of single actin filaments in vitro. , 1996, Biophysical chemistry.

[3]  J. Spudich,et al.  The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. , 1971, The Journal of biological chemistry.

[4]  T. Yanagida,et al.  Orientation dependence of displacements by a single one-headed myosin relative to the actin filament. , 1998, Biophysical journal.

[5]  E. Reisler [10] Sulfhydryl modification and labeling of myosin , 1982 .

[6]  J. Sellers,et al.  Polarity and velocity of sliding filaments: control of direction by actin and of speed by myosin. , 1990, Science.

[7]  A. Huxley,et al.  The variation in isometric tension with sarcomere length in vertebrate muscle fibres , 1966, The Journal of physiology.

[8]  J. Wakayama,et al.  Contractility of single myofibrils of rabbit skeletal muscle studied at various MgATP concentrations. , 2000, The Japanese journal of physiology.

[9]  T. Yanagida,et al.  Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. , 1990, Journal of molecular biology.

[10]  S. Lowey,et al.  [7] Preparation of myosin and its subfragments from rabbit skeletal muscle , 1982 .

[11]  S. Ishiwata,et al.  Preparation of bead-tailed actin filaments: estimation of the torque produced by the sliding force in an in vitro motility assay. , 1996, Biophysical journal.

[12]  T. Wakabayashi,et al.  Movement of actin away from the center of reconstituted rabbit myosin filament is slower than in the opposite direction. , 1993, Biophysical Journal.

[13]  A. Yagi,et al.  Transverse elasticity of myofibrils of rabbit skeletal muscle studied by atomic force microscopy. , 1999, Biochemical and biophysical research communications.

[14]  S. Ishiwata,et al.  Right-handed rotation of an actin filament in an in vitro motile system , 1993, Nature.

[15]  H Nakayama,et al.  Fine profile of actomyosin motility fluctuation revealed by using 40-nm probe beads. , 1998, Biochemical and biophysical research communications.

[16]  J. Squire The Structural Basis of Muscular Contraction , 1981, Springer US.

[17]  James A. Spudich,et al.  Myosin subfragment-1 is sufficient to move actin filaments in vitro , 1987, Nature.