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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Processive movement of single 22S dynein molecules occurs only at low ATP concentrations
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Processive movement of single 22S dynein molecules occurs only at low ATP concentrations

机译：单个22S动力蛋白分子的进行性运动仅在低ATP浓度下发生

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摘要

We have analyzed the movement of single 22S dynein molecules from Tetrahymena cilia by using a nanometer measuring system equipped with optical tweezers. Statistical analysis proved that a single molecule of 22S dynein can move processively and develop force at low concentrations of ATP (<20 HM). The maximum force was ≈4.7 pN, and the force-velocity curve was convex down. During force development. dynein molecules showed stepwise displacement of ≈8 nm and frequently exhibited backward steps of ≈8 nm. At higher concentrations of ATP (g20 pM) single molecules of 22S dynein were not observed to move processively. Twenty-two S dynein seems to switch over from a processive mode to a nonprocessive mode. sensing a subtle change of ATP concen- trations. These observations indicate that the processivity, maxi- mum force, and step size of dynein are similar to those of kinesin, but the ATP concentration-dependence, force-velocity relation- ship. and backward steps are clearly distinct from kinesin.
机译：我们已经通过使用配备有光镊子的纳米测量系统分析了四膜虫纤毛中单个22S动力蛋白的运动。统计分析证明，单分子22S动力蛋白可进行性移动并在低浓度ATP（<20 HM）下产生作用力。最大力为≈4.7pN，力-速度曲线向下凸。在部队发展期间。动力蛋白分子显示出约8 nm的逐步位移，并经常表现出约8 nm的后退台阶。在较高浓度的ATP（g20 pM）下，未观察到22S动力蛋白的单分子进行性移动。 22个S达因似乎从过程模式转换为非过程模式。感觉到ATP浓度的细微变化。这些观察结果表明，动力蛋白的合成能力，最大作用力和步长与驱动蛋白相似，但ATP浓度依赖性，作用力-速度关系。后退步骤显然不同于驱动蛋白。

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