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首页> 外文期刊>Journal of Molecular Biology >KINESIN AND NCD BIND THROUGH A SINGLE HEAD TO MICROTUBULES AND COMPETE FOR A SHARED MT BINDING SITE
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KINESIN AND NCD BIND THROUGH A SINGLE HEAD TO MICROTUBULES AND COMPETE FOR A SHARED MT BINDING SITE

机译：驱动蛋白和NCD通过单头结合到微管上并竞争共享的MT绑定站点

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摘要

Kinesin and non claret disjunctional are closely related molecular motors that move in opposite directions along microtubules. We have used recombinant single-headed and double-headed constructs of both rat kinesin heavy chain and non claret disjunctional to investigate the interactions of these motor proteins with microtubules. At saturation the stoichiometry of binding for non claret disjunctional and kinesin to microtubules is one molecule (single or double-headed) per tubulin heterodimer. In the absence of added nucleotide, addition of increasing amounts of one motor results in the competitive displacement of the other motor from the microtubules. This effect is apparent also in the presence of the nucleotide analogue 5'-adenylimidodiphosphate, which tightens the binding of both kinesin and non claret disjunctional. Competition for binding sites occurs also under conditions of steady-state ATP turnover. We conclude that despite their opposite directionality, kinesin and non claret disjunctional compete for overlapping binding sites on the MT surface. Since the binding of the second head of a double-headed motor is sterically blocked, the data imply also that both kinesin and non claret disjunctional may translocate via a processive (alternating heads) mechanism with a minimum step size of similar to 8 nm. [References: 27]
机译：驱动蛋白和非紫红色分离蛋白是紧密相关的分子马达，它们沿着微管以相反的方向移动。我们已经使用大鼠驱动蛋白重链和非紫红色分离的重组单头和双头构建体来研究这些运动蛋白与微管的相互作用。非紫红色分离蛋白和驱动蛋白与微管结合的化学计量为每个微管蛋白异二聚体一个分子（单头或双头）。在不存在添加的核苷酸的情况下，增加数量的一种运动的添加导致另一种运动从微管的竞争性置换。在核苷酸类似物5'-腺苷亚氨基二磷酸的存在下，这种作用也很明显，该核苷酸类似物加强了驱动蛋白和非紫红色分离的结合。结合位点的竞争也在稳态ATP转换的条件下发生。我们得出结论，尽管它们的方向性相反，但驱动蛋白和非紫红色析取物竞争MT表面上的重叠结合位点。由于双头电机的第二个头的结合在空间上受阻，因此数据还暗示驱动蛋白和非紫红色分离蛋白都可以通过过程性（交替头）机制转移，最小步长类似于8 nm。 [参考：27]

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