Vale R D, Toyoshima Y Y
Department of Pharmacology, University of California, San Francisco 94143.
Cell. 1988 Feb 12;52(3):459-69. doi: 10.1016/s0092-8674(88)80038-2.
Dynein, the force-generating enzyme that powers the movement of cilia and flagella, has been characterized biochemically, but no simple system has been available for examining its motile properties. Here we describe a quantitative in vitro motility assay in which dynein adsorbed onto a glass surface induces linear translocation of purified bovine microtubules. Using this assay, we show that both 22S and 14S dyneins from Tetrahymena cilia induce movement but have distinct motile properties. A unique property of 14S dynein, which has not been described for other motility proteins, is its ability to generate torque that causes microtubules to rotate during forward translocation. In the axoneme, 14S dynein-induced torque may induce rotation of central-pair microtubules and may play an important role in generating three-dimensional ciliary beating patterns.
动力蛋白是一种为纤毛和鞭毛运动提供动力的产生力的酶，已通过生物化学方法进行了表征，但尚无简单系统可用于研究其运动特性。在此，我们描述了一种定量体外运动分析方法，其中吸附在玻璃表面的动力蛋白可诱导纯化的牛微管进行线性移位。使用该分析方法，我们发现来自四膜虫纤毛的22S和14S动力蛋白均可诱导运动，但具有不同的运动特性。14S动力蛋白具有一种其他运动蛋白未被描述过的独特特性，即其能够产生扭矩，使微管在向前移位时发生旋转。在轴丝中，14S动力蛋白诱导的扭矩可能会诱导中央微管对发生旋转，并可能在产生三维纤毛跳动模式中发挥重要作用。
