Stewart R J, Thaler J P, Goldstein L S
Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138.
Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5209-13. doi: 10.1073/pnas.90.11.5209.
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.
果蝇的驱动蛋白重链和ncd(非红化分离)基因产物是微管相关的运动蛋白,在大约340个氨基酸的结构域内具有序列相似性。尽管存在序列相似性,但驱动蛋白重链和ncd蛋白在微管上沿相反方向移动。为了研究运动方向的分子基础,我们构建了一系列截短的驱动蛋白重链和ncd蛋白。我们发现,两种蛋白的保守结构域都具有微管运动活性,尽管ATP水解与微管运动偶联的效率随着截短程度的增加而急剧下降。此外,运动方向是保守运动结构域所固有的,而不是结构域组织或相邻序列的结果。