Bi‐directional movement of actin filaments along long bipolar tracks of oriented rabbit skeletal muscle myosin molecules

FEBS Letters

Yamada, Akira¹  Nakayama, Haruto¹  Yoshio, Maki¹ 

[1] Kansai Advanced Research Center, Communications Research Laboratory, Iwaoka-cho, Nishi-ku, Kobe 651-24, Japan

关键词: Myosin;    Actin;    In vitro motility assay;    Myosin rod;    Molluscan smooth muscle;    PIPES;    piperazine-N;    N′-bis(2-ethanesulfonic acid);    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide electrophoresis;    BSA;    bovine serum albumin;    DTT;    dithiothreitol;    ABRM;    anterior byssus retractor muscle;    PBRM;    posterior byssus retractor muscle;    PAM;    posterior adductor muscle;   

DOI  :  10.1016/S0014-5793(97)00558-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In actomyosin in vitro motility assays, orientation of myosin molecules affects their interaction with actin. We obtained long tracks of myosin molecules with uniform orientation. Bipolar filaments about 50 μm long were made from myosin rod prepared from molluscan smooth muscles, to which rabbit skeletal-muscle myosin bound, creating long synthetic thick-filaments. Movement of F-actin toward their center was much faster (4.7±0.6 μm s⁻¹) than in the opposite direction (1.9±0.2 μm s⁻¹), indicating that myosin molecules were arranged in the same orientation along each half of the bipolar filament. These complex thick-filaments permit measurement of actin movement over 20 μm of oriented skeletal myosin tracks facilitating mechanistic studies of actomyosin motility.

【 授权许可】

Unknown