Protein components of ribonucleoprotein granules from Drosophila germ cells oligomerize and show distinct spatial organization during germline development

Protein components of ribonucleoprotein granules from Drosophila germ cells oligomerize and show distinct spatial organization during germline development
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DOI:
10.1038/s41598-019-55747-x
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发表时间:
2019-12
期刊:
影响因子:
4.6
通讯作者:
Hieu D. L. Vo;Wahiduzzaman;Samuel J. Tindell;Jimiao Zheng;Ming Gao;A. Arkov
Hieu D. L. Vo;Wahiduzzaman;Samuel J. Tindell;Jimiao Zheng;Ming Gao;A. Arkov
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Hieu D. L. Vo;Wahiduzzaman;Samuel J. Tindell;Jimiao Zheng;Ming Gao;A. Arkov

文献摘要

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大RNA-蛋白质颗粒的组装发生在许多动物的生殖细胞中,并且这些生殖颗粒提供了研究不同细胞中相似结构的结构-功能方面的范例。果蝇胚细胞后极的生殖颗粒(极性颗粒)由RNA和生殖细胞发育所需的蛋白质组成。在颗粒中,Piwi蛋白Aubergine与支架蛋白Tudor结合,该支架蛋白含有11个Tudor结构域。使用超分辨率显微镜,我们发现,令人惊讶的是,Aubergine和Tudor形成不同的集群内相同的极性颗粒在earlyDrosophila胚胎。这些簇部分重叠,在生殖细胞形成后,它们转变成球形颗粒,其结构组织与这些相互作用的蛋白质意想不到:都铎核心周围的茄子壳。与形成不同的集群一致,我们表明,茄子形成同源寡聚物,并使用所有纯化的都铎结构域,我们证明了多个域,分布沿着整个都铎结构,与茄子相互作用。我们的数据表明,在极性颗粒中,茄子和Tudor组装成不同的相,在其“相互作用中心”部分混合,并且不同蛋白质簇的结合可能是胚芽颗粒组装的进化保守机制。
The assembly of large RNA-protein granules occurs in germ cells of many animals and these germ granules have provided a paradigm to study structure-functional aspects of similar structures in different cells. Germ granules inDrosophilaoocyte’s posterior pole (polar granules) are composed of RNA, in the form of homotypic clusters, and proteins required for germline development. In the granules, Piwi protein Aubergine binds to a scaffold protein Tudor, which contains 11 Tudor domains. Using a super-resolution microscopy, we show that surprisingly, Aubergine and Tudor form distinct clusters within the same polar granules in earlyDrosophilaembryos. These clusters partially overlap and, after germ cells form, they transition into spherical granules with the structural organization unexpected from these interacting proteins: Aubergine shell around the Tudor core. Consistent with the formation of distinct clusters, we show that Aubergine forms homo-oligomers and using all purified Tudor domains, we demonstrate that multiple domains, distributed along the entire Tudor structure, interact with Aubergine. Our data suggest that in polar granules, Aubergine and Tudor are assembled into distinct phases, partially mixed at their “interaction hubs”, and that association of distinct protein clusters may be an evolutionarily conserved mechanism for the assembly of germ granules.