Flexibility in actin-myosin motility system revealed by in vitro motility assay.
Flexibility of myosin molecule was studied by in vitro motility assay in terms of the direction of actin movement. Electron microscopy showed that HMM scattered on a nitrocellulose surface can bind actin filaments and form arrowhead-like patterns. Actin filaments can move in both directions on tracks of HMM made on a nitrocellulose surface. Further, actin filaments can move bidirectionally along native thick filaments over their central bare zone. These observations indicate that there is considerable flexibility in a myosin molecule and that the direction of the movement is determined by the polarity of actin filaments.
Toyoshima
Y Y
YY
Department of Biology, Ochanomizu University, Tokyo, Japan.
D000199:Actins / Q000502:physiology* / Q000648:ultrastructure; D000818:Animals; D008854:Microscopy, Electron / Q000379:methods; D009068:Movement; D009119:Muscle Contraction; D015879:Myosin Subfragments / Q000502:physiology* / Q000648:ultrastructure; D011485:Protein Binding
D000199:Actins; D015879:Myosin Subfragments