Direction of microtubule movement is an intrinsic property of the motor domains of kinesin heavy chain and Drosophila ncd protein.
Direction of microtubule movement is an intrinsic property of the motor domains of kinesin heavy chain and Drosophila ncd protein.
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微管运动方向是驱动蛋白重链和果蝇 ncd 蛋白运动结构域的固有特性。
DOI：
10.1073/pnas.90.11.5209
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发表时间：
1993
影响因子：
11.1
通讯作者：
Lawrence S. B. Goldstein
中科院分区：
文献类型：
--
作者：
Russell J. Stewart;Joshua P. Thaler;Lawrence S. B. Goldstein
果蝇的驱动蛋白重链和 ncd（非紫红色分离）基因产物是微管相关运动蛋白，在大约 340 个氨基酸的结构域内通过序列相似性相关。尽管序列相似，驱动蛋白重链和 ncd 蛋白在微管上的移动方向相反。为了研究运动方向的分子基础，我们创建了一系列截短的驱动蛋白重链和 ncd 蛋白。我们发现这两种蛋白质的保守结构域都具有微管运动活性，尽管 ATP 水解与微管运动耦合的效率随着截断的增加而急剧下降。此外，运动方向是保守运动域固有的，而不是域组织或相邻序列的结果。
The kinesin heavy chain and the ncd (non-claret disjunctional) gene product of Drosophila are microtubule-associated motor proteins related by sequence similarity within an approximately 340-aa domain. Despite the sequence similarity, the kinesin heavy chain and ncd protein move in opposite directions on microtubules. To investigate the molecular basis for direction of movement, we created a series of truncated kinesin heavy chain and ncd proteins. We found that the conserved domain of both proteins has microtubule motor activity, although the efficiency with which ATP hydrolysis is coupled to microtubule movement declines dramatically with increasing truncation. Further, the direction of movement is intrinsic to the conserved motor domains, rather than being a consequence of domain organization or adjacent sequences.