Toyoshima Y Y, Toyoshima C, Spudich J A
Department of Cell Biology, Stanford University School of Medicine, California 94305.
Nature. 1989 Sep 14;341(6238):154-6. doi: 10.1038/341154a0.
It is well established that muscle contraction results from the relative sliding of actin and myosin filaments. Both filaments have definite polarities and well-ordered structures. Thick filaments, however, are not vital for supporting movement in vitro. Previously we have demonstrated that actin filaments can move continuously on myosin fragments (subfragment-1 or heavy meromyosin (HMM] that are bound to a nitrocellulose surface. Here we report that actin filaments can move in opposite directions on tracks of myosin heads formed when actin filaments decorated with HMM are placed on a nitrocellulose surface. The actin filaments always move forward, frequently changing the direction of the movement, but never move backward reversing the polarity of the movement. The direction of movement is therefore determined by the polarity of the actin filament. These results indicate that myosin heads have considerable flexibility.
众所周知,肌肉收缩是由肌动蛋白丝和肌球蛋白丝的相对滑动引起的。这两种丝都具有确定的极性和有序的结构。然而,粗丝对于体外支持运动并非至关重要。此前我们已经证明,肌动蛋白丝可以在结合到硝酸纤维素表面的肌球蛋白片段(亚片段-1或重酶解肌球蛋白(HMM))上连续移动。在此我们报告,当用HMM修饰的肌动蛋白丝放置在硝酸纤维素表面时,肌动蛋白丝可以在由肌球蛋白头部形成的轨道上沿相反方向移动。肌动蛋白丝总是向前移动,频繁改变运动方向,但从不向后移动从而逆转运动的极性。因此,运动方向由肌动蛋白丝的极性决定。这些结果表明,肌球蛋白头部具有相当大的灵活性。