An evolutionarily conserved SSNA1/DIP13 homologue is a component of both basal and apical complexes of Toxoplasma gondii.
An evolutionarily conserved SSNA1/DIP13 homologue is a component of both basal and apical complexes of Toxoplasma gondii.
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DOI：
10.1038/srep27809
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发表时间：
2016-06-21
影响因子：
4.6
通讯作者：
Besteiro S
中科院分区：
文献类型：
--
作者：
Lévêque MF;Berry L;Besteiro S
基于微管的细胞骨架结构在几个重要的真核生物过程中起着重要作用，包括细胞内成分的运输以及纤毛和鞭毛的流动性。微管的时间和空间组织由微管组织中心和许多附属物和辅助蛋白决定。SSNA 1/DIP 13家族的成员是卷曲螺旋蛋白，已知其定位于微管结构如中心体和鞭毛，但在其他方面表征不佳。我们已经确定了SSNA 1/DIP 13的同源物在寄生原生动物弓形虫，并发现它定位于寄生虫特异性的细胞骨架结构：圆锥体的顶端复杂的成熟和分裂的细胞，和基础复杂的延长子细胞在细胞分裂过程中。这种蛋白质在体外对寄生虫生长有抑制作用。然而，非常值得注意的是，这种卷曲螺旋蛋白能够在体外和体内自缔合成更高级的结构，并且其过表达损害寄生虫分裂。
Microtubule-based cytoskeletal structures have fundamental roles in several essential eukaryotic processes, including transport of intracellular constituents as well as ciliary and flagellar mobility. Temporal and spatial organisation of microtubules is determined by microtubule organising centers and a number of appendages and accessory proteins. Members of the SSNA1/DIP13 family are coiled coil proteins that are known to localise to microtubular structures like centrosomes and flagella, but are otherwise poorly characterised. We have identified a homologue of SSNA1/DIP13 in the parasitic protist Toxoplasma gondii and found it localises to parasite-specific cytoskeletal structures: the conoid in the apical complex of mature and dividing cells, and the basal complex in elongating daughter cells during cell division. This protein is dispensable for parasite growth in vitro. However, quite remarkably, this coiled coil protein is able to self-associate into higher order structures both in vitro and in vivo, and its overexpression is impairing parasite division.