Grummt M, Pistor S, Lottspeich F, Schliwa M
Adolf-Butenandt-Institut, Zellbiologie, University of Munich, Germany.
FEBS Lett. 1998 May 1;427(1):79-84. doi: 10.1016/s0014-5793(98)00399-8.
Conventional kinesins are molecular motors that move towards the plus end of microtubules. In animal species, they have been shown to be remarkably conserved in terms of both their primary sequence and several physiological properties, including their velocity of movement. Here we report the cloning of Synkin, a homologue of conventional kinesin from the zygomycete fungus Syncephalastrum racemosum [Steinberg, Eur. J. Cell Biol. 73 (1997) 124-131] that is 4-5 times faster than its animal counterparts. Expression in bacteria yields a fully functional motor that moves at the same speed as the native motor isolated from fungal hyphae and has similar hydrodynamic properties. Its sequence is most closely related to that of two other fungal kinesins from Neurospora and Ustilago, and shares several biochemical properties with the Neurospora motor. Fungal kinesins therefore seem to form a conserved subfamily of conventional kinesins distantly related to animal kinesins. They may help to identify sequence features important for determining motor velocity.
传统驱动蛋白是朝着微管正端移动的分子马达。在动物物种中,它们在一级序列和包括移动速度在内的多种生理特性方面都表现出显著的保守性。在此,我们报告了来自接合菌纲真菌总状共头霉([施泰因贝格,《欧洲细胞生物学杂志》73 (1997) 124 - 131])的传统驱动蛋白同源物Synkin的克隆,其移动速度比动物同类快4至5倍。在细菌中表达产生了一种功能完全的马达,其移动速度与从真菌菌丝体中分离出的天然马达相同,并且具有相似的流体动力学特性。它的序列与来自粗糙脉孢菌和黑粉菌的另外两种真菌驱动蛋白的序列关系最为密切,并且与粗糙脉孢菌的马达具有若干生化特性。因此,真菌驱动蛋白似乎构成了与动物驱动蛋白远缘相关的传统驱动蛋白的一个保守亚家族。它们可能有助于识别对于确定马达速度重要的序列特征。