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首页> 外文期刊>Journal of cell biology >A single-headed fission yeast myosin V transports actin in a tropomyosin-dependent manner
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A single-headed fission yeast myosin V transports actin in a tropomyosin-dependent manner

机译:单头裂殖酵母肌球蛋白V以原肌球蛋白依赖性方式转运肌动蛋白

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摘要

Myo51, a class V myosin in fission yeast, localizes to and assists in the assembly of the contractile ring, a conserved eukaryotic actomyosin structure that facilitates cytokinesis. Rng8 and Rng9 are binding partners that dictate the cellular localization and function of Myo51. Myo51 was expressed in insect cells in the presence or absence of Rng8/9. Surprisingly, electron microscopy of negatively stained images and hydrodynamic measurements showed that Myo51 is single headed, unlike most class V myosins. When Myo51–Rng8/9 was bound to actin-tropomyosin, two attachment sites were observed: the typical ATP-dependent motor domain attachment and a novel ATP-independent binding of the tail mediated by Rng8/9. A modified motility assay showed that this additional binding site anchors Myo51–Rng8/9 so that it can cross-link and slide actin-tropomyosin filaments relative to one another, functions that may explain the role of this motor in contractile ring assembly.
机译:Myo51是裂变酵母中的V类肌球蛋白,它定位并协助收缩环的组装,该收缩环是一种保守的真核肌动球蛋白结构,有助于胞质分裂。 Rng8和Rng9是决定Myo51的细胞定位和功能的结合伴侣。在有或没有Rng8 / 9的情况下,Myo51在昆虫细胞中表达。出乎意料的是,与大多数V类肌球蛋白不同,负染色图像的电子显微镜和流体动力学测量表明Myo51是单头的。当Myo51–Rng8 / 9与肌动蛋白原肌球蛋白结合时,观察到两个附着位点:典型的ATP依赖性运动域附着和由Rng8 / 9介导的尾巴的新型ATP依赖性结合。一种改进的运动分析表明,这种额外的结合位点可锚定Myo51–Rng8 / 9,使其可以相互交联并使肌动蛋白原肌球蛋白丝彼此相对滑动,其功能可能解释了这种运动在收缩环组装中的作用。

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