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首页> 外文期刊>Journal of Molecular Biology >Complex formation with Kinesin motor domains affects the structure of microtubules.
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Complex formation with Kinesin motor domains affects the structure of microtubules.

机译：与驱动蛋白运动域的复合物形成影响微管的结构。

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摘要

Microtubules are highly dynamic components of the cytoskeleton. They are important for cell movement and they are involved in a variety of transport processes together with motor proteins, such as kinesin. The exact mechanism of these transport processes is not known and so far the focus has been on structural changes within the motor domains, but not within the underlying microtubule structure.Here we investigated the interaction between kinesin and tubulin and our experimental data show that microtubules themselves are changing structure during that process. We studied unstained, vitrified samples of microtubules composed of 15 protofilaments using cryo electron microscopy and helical image analysis. 3D maps of plain microtubules and microtubules decorated with kinesin have been reconstructed to approximately 17A resolution. The alphabeta-tubulin dimer could be identified and, according to our data, alpha- and beta-tubulin adopt different conformations in plain microtubules. Significant differences were detected between maps of plain microtubules and microtubule-kinesin complexes. Most pronounced is the continuous axial inter-dimer contact in the microtubule-kinesin complex, suggesting stabilized protofilaments along the microtubule axis. It seems, that mainly structural changes within alpha-tubulin are responsible for this observation. Lateral effects are less pronounced. Following our data, we believe, that microtubules play an active role in intracellular transport processes through modulations of their core structure.
机译：微管是细胞骨架的高度动态成分。它们对于细胞运动很重要，并且与运动蛋白（例如驱动蛋白）一起参与多种转运过程。这些转运过程的确切机制尚不清楚，到目前为止，焦点一直集中在运动域内的结构变化，而不是潜在的微管结构内。这里我们研究了驱动蛋白和微管蛋白之间的相互作用，我们的实验数据表明微管本身在此过程中正在改变结构。我们使用冷冻电子显微镜和螺旋图像分析研究了由15条原丝组成的未染色的玻璃化微管样品。普通微管和用驱动蛋白修饰的微管的3D图已重建到大约17A分辨率。可以识别字母微管蛋白二聚体，根据我们的数据，α-和β-微管蛋白在普通微管中采用不同的构象。在普通微管和微管-驱动蛋白复合物的图谱之间检测到显着差异。最明显的是在微管-驱动蛋白复合物中的连续的轴向二聚体间接触，表明沿微管轴的稳定的原丝。看来，α-微管蛋白内部的主要结构变化是造成这种观察的原因。横向影响不太明显。根据我们的数据，我们认为，微管通过调节其核心结构在细胞内转运过程中发挥了积极作用。

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