Structural and functional analysis of novel dyneins localized to the ciliary proximal region

我们分析了次要动力蛋白的结构和功能，它们的轴突含量低于其他主要动力蛋白。在这里，我们发现三种次要动力蛋白中的一种比大多数衣藻动力蛋白在缺乏ATP的情况下与微管的结合更强。此外，使用低温电子断层扫描和亚断层扫描平均，我们发现每个次要动力蛋白都位于睫状近端区域，而不是特定的主要动力蛋白。此外，我们还发现了一种新的巨大动力蛋白，这是衣藻中最后一个有待鉴定的动力蛋白重链，它位于9个双重微管中的一个的近端区域。这是首次在单一生物中鉴定出动力蛋白重链的所有基因产物。

We analyzed the structure and function of minor-type dyneins whose axonemal contents are lower than other major-type dyneins. Here we found that one of three minor dyneins more strongly bind to microtubules than most of Chlamydomonas dyneins in the absence of ATP. In addition, using cryoelectron tomography and subtomogram averaging, we found that each minor dynein locates to the ciliary proximal region in place of a specific major dynein. Furthermore, we found that a novel gigantic dynein, which has been the last dynein heavy chain remained to be identified in Chlamydomonas, localizes to the proximal region of one of nine doublet microtubules. This is the first report that all the gene products of dynein heavy chain have been identified in the singleorganism.