title: Flexibility in actin-myosin motility system revealed by in vitro motility assay.
abstract: 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.
authors.affiliation: Department of Biology, Ochanomizu University, Tokyo, Japan.
authors.forename: Y Y
authors.initials: YY
authors.lastname: Toyoshima
mesh_terms: 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
chemical_list: D000199:Actins; D015879:Myosin Subfragments