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首页> 外文期刊>Journal of Muscle Research and Cell Motility >Visualization of caldesmon binding to synthetic filaments of smooth muscle myosin.
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Visualization of caldesmon binding to synthetic filaments of smooth muscle myosin.

机译:可视化卡尔德斯蒙与平滑肌肌球蛋白合成丝的结合。

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摘要

We have used synthetic filaments of unphosphorylated chicken gizzard myosin with a compact, highly ordered structure under relaxing conditions (in the absence of Ca2+ and in the presence of ATP) to visualize the mode of caldesmon binding to myosin filaments by negative staining and immunogold electron microscopy. We demonstrate that the addition of caldesmon to preformed myosin filaments leads to the appearance of numerous smooth projections curving out from the filament surface. The addition of caldesmon or its N-terminal fragment resulted in the partial masking of myosin filament periodicity. However, it did not change the inner structure of the filaments. It is demonstrated that most caldesmon molecules bind to myosin filaments through the N-terminal part, while the C-terminal parts protrude from the filament surface, as confirmed by immunoelectron microscopy visualization. Together with the available biochemical data on caldesmon binding to both actin and myosin and electron microscopic observations on the mode of caldesmon attachment to actin filaments with the C-termini of the molecules curving out from the filaments, the visualization of caldesmon attachment to myosin filaments completes the scenario of actin to myosin tethering by caldesmon.
机译:我们已经使用了在松弛条件下(无Ca2 +和ATP的情况下)具有紧凑,高度有序结构的未磷酸化鸡g肌球蛋白的合成细丝,通过负向染色和免疫金电子显微镜观察了卡尔德斯蒙与肌球蛋白细丝的结合模式。我们证明向预成型的肌球蛋白细丝中添加卡尔德斯蒙导致从细丝表面弯曲的许多平滑凸起的出现。 Caldesmon或其N末端片段的添加导致肌球蛋白丝周期的部分掩盖。但是,它并没有改变细丝的内部结构。免疫电子显微镜观察证实,多数卡尔德斯蒙分子都通过N端部分与肌球蛋白丝结合,而C端部分则从丝表面突出。连同有关肌钙蛋白与肌动蛋白和肌球蛋白结合的可用生化数据以及关于肌钙蛋白与肌动蛋白细丝的附着方式以及分子从细丝弯曲的C末端的电子显微镜观察,完成了对肌钙蛋白与肌球蛋白细丝的附着的可视化肌动蛋白与肌球蛋白之间由Caldesmon进行连接的情况。

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