Functions and mechanics of dynein motor proteins.

Functions and mechanics of dynein motor proteins.
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DOI:
10.1038/nrm3667
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发表时间:
2013-11
期刊:
Nature reviews. Molecular cell biology
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在 ATP 水解的推动下,动力蛋白在纤毛跳动、细胞分裂和细胞内运输等丰富的生物过程中在微管上产生力和运动。动力蛋白电机的巨大质量和复杂性使得阐明其机制成为一项艰巨的任务。然而,通过结合 X 射线晶体学、冷冻电子显微镜、单分子测定和生化实验等方法,在了解这些巨型运动蛋白的工作原理方面已经取得了重要进展。从这些研究中,动力蛋白机械化学循环的模型正在出现,其中动力蛋白 AAA+ 环内核苷酸驱动的弯曲运动改变其微管结合柄的亲和力并重塑其机械元件以产生运动。
Fuelled by ATP hydrolysis, dyneins generate force and movement on microtubules in a wealth of biological processes, including ciliary beating, cell division and intracellular transport. The large mass and complexity of dynein motors have made elucidating their mechanisms a sizable task. Yet, through a combination of approaches, including X-ray crystallography, cryo-electron microscopy, single-molecule assays and biochemical experiments, important progress has been made towards understanding how these giant motor proteins work. From these studies, a model for the mechanochemical cycle of dynein is emerging, in which nucleotide-driven flexing motions within the AAA+ ring of dynein alter the affinity of its microtubule-binding stalk and reshape its mechanical element to generate movement.
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