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首页> 外文期刊>Cytoskeleton >Structure of dimeric axonemal dynein in cilia suggests an alternative mechanism of force generation
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Structure of dimeric axonemal dynein in cilia suggests an alternative mechanism of force generation

机译：纤毛中二聚体轴索动力蛋白的结构表明产生力的另一种机制

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The mechanism by which the two different heads of the ciliary outer dynein arm produce force to translocate the microtubule during beating is still unknown. In this report we use cryo-electron tomography and image processing to analyze the conformational changes and the relative abundance of each conformation of the two dynein heads from mouse respiratory cilia. In the absence of nucleotides the majority of dynein dimers are in the apo form and both heads are tightly packed, whereas they are dissociated and move independently in the presence of nucleotides. The head of the external outer arm dynein heavy chain has a diagonal shift toward both the neighboring B-tubule and the proximal end of the axoneme, while the head of the internal heavy chain shifts only longitudinally toward the proximal end. In the presence of nucleotides a significant number of the dynein dimers have two heads overlapped in the proximal shifting form or overlapped in the apo form. During ciliary bending axonemal dynein translocates microtubules by moving with short steps and two heads stay at the same position longer than cytoplasmic dynein. This demonstrates that the step of the outer arm dynein dimer is not dominated by the hand-over-hand motion, but also indicates the difference between axonemal dynein and cytoplasmic dynein.
机译：睫状外达因臂的两个不同头部在跳动过程中产生力使微管移位的机制仍然未知。在本报告中，我们使用冷冻电子断层扫描和图像处理技术来分析小鼠呼吸性纤毛的两个达因素头的构象变化和每种构象的相对丰度。在缺乏核苷酸的情况下，大多数达因二聚体呈载脂蛋白形式，并且两个头部紧密堆积，而在存在核苷酸的情况下，它们分离并独立移动。外部外臂动力蛋白重链的头部向相邻的B小管和轴突的近端都有一个对角线移位，而内部重链的头部仅向近端纵向移动。在存在核苷酸的情况下，大量的达因二聚体具有两个头以近端移位形式重叠或以载脂蛋白形式重叠。在睫状体弯曲过程中，轴索动力蛋白通过短步移动而使微管移位，并且两个头部在同一位置停留的时间比细胞质动力蛋白更长。这表明外臂动力蛋白二聚体的步移不由交接动作决定，但也表明了轴突动力蛋白与胞质动力蛋白之间的差异。

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