title: Right-handed rotation of an actin filament in an in vitro motile system.
abstract: Muscle contraction occurs by mutual sliding between thick (myosin) and thin (actin) filaments. But the physical and chemical properties of the sliding force are not clear; even the precise direction of sliding force generated at each cross-bridge is not known. We report here the use of a recently developed in vitro motile assay system to show supercoiling of an actin filament in which the front part of the filament was fixed to a glass surface through cross-linked heavy-meromyosin and the rear part was able to slide on a track of heavy-meromyosin. A left-handed single turn of superhelix formed just before supercoiling, suggesting that the sliding force has a right-handed torque component that induces the right-handed rotation of an actin filament around its long axis. The presence of the torque component in the sliding force will explain several properties of the contractile system of muscle.
authors.affiliation: Department of Physics, School of Science and Engineering, Waseda University, Tokyo, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Nishizaka
authors.forename: T
authors.initials: T
authors.lastname: Yagi
authors.forename: Y
authors.initials: Y
authors.lastname: Tanaka
authors.forename: S
authors.initials: S
authors.lastname: Ishiwata
mesh_terms: D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D003432:Cross-Linking Reagents; D004229:Dithiothreitol; D005033:Ethylmaleimide; D008961:Models, Structural; D009119:Muscle Contraction; D015879:Myosin Subfragments / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D012399:Rotation
chemical_list: D000199:Actins; D003432:Cross-Linking Reagents; D015879:Myosin Subfragments; D005033:Ethylmaleimide; D004229:Dithiothreitol