Nishizaka T, Yagi T, Tanaka Y, Ishiwata S
Department of Physics, School of Science and Engineering, Waseda University, Tokyo, Japan.
Nature. 1993 Jan 21;361(6409):269-71. doi: 10.1038/361269a0.
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.
肌肉收缩是由粗肌丝(肌球蛋白)和细肌丝(肌动蛋白)之间的相互滑动引起的。但是,滑动力的物理和化学性质尚不清楚;甚至每个横桥产生的滑动力的确切方向也未知。我们在此报告使用最近开发的体外运动分析系统来展示肌动蛋白丝的超螺旋,其中肌动蛋白丝的前部通过交联的重酶解肌球蛋白固定在玻璃表面,而后部能够在重酶解肌球蛋白的轨道上滑动。在超螺旋形成之前会形成一个左旋单圈超螺旋,这表明滑动力具有一个右旋扭矩分量,该分量会诱导肌动蛋白丝围绕其长轴进行右旋旋转。滑动力中扭矩分量的存在将解释肌肉收缩系统的几个特性。