Characterization of Tudor-sn-containing granules in the silkworm, Bombyx mori.
Characterization of Tudor-sn-containing granules in the silkworm, Bombyx mori.
复制标题
DOI：
10.1016/j.ibmb.2013.04.004
复制
发表时间：
2013-08
影响因子：
3.8
通讯作者：
Li Zhu;Tsuneyuki Tatsuke;H. Mon;Zhiqing Li;Jian Xu;J. M. Lee;T. Kusakabe
中科院分区：
文献类型：
--
作者：
Li Zhu;Tsuneyuki Tatsuke;H. Mon;Zhiqing Li;Jian Xu;J. M. Lee;T. Kusakabe
Tudor-sn蛋白含有四个葡萄球菌核酸酶结构域和一个Tudor结构域，是一种几乎在所有生物体中都存在的蛋白质。已有研究报道，哺乳动物中的Tudor-sn参与多种细胞通路，参与基因调控、细胞生长和发育。在昆虫中，我们已经在家蚕中发现了一个Tudor-sn同源基因，并检测到它与ArgAerte蛋白之间的相互作用。然而，都铎-sn在家蚕中的作用在很大程度上仍然是未知的。在本研究中，我们证实了家蚕Tudor-sn是一种应激颗粒蛋白，并用双分子荧光互补分析和昆虫双杂交方法确定了其与其他应激颗粒蛋白的相互作用。RNAi缺失ArgAerte蛋白和SG标记蛋白Tia1，削弱了Tudor-sn在SG形成中的参与。对Tudor-sn的蛋白质结构域缺失分析表明，SN2是Tudor-sn在SGS中聚集所需的关键域。
The Tudor-sn protein, which contains four staphylococcal nuclease domains and a Tudor domain, is a ubiquitous protein found in almost all organisms. It has been reported that Tudor-sn in mammals participates in various cellular pathways involved in gene regulation, cell growth, and development. In insects, we have previously identified a Tudor-sn ortholog in the silkworm,Bombyx mori, and detected its interactions between with Argonaute proteins. The role of Tudor-sn in silkworm, however, still remains largely unknown. In this study, we demonstrated that silkworm Tudor-sn is a stress granule (SG) protein, and determined its interactions with other SG proteins using Bimolecular Fluorescence Complementation assay and Insect Two-Hybrid method. Depletions of Argonaute proteins and SG-marker protein Tia1 by RNAi impaired the involvement of Tudor-sn in the SG formation. Protein domain deletion analysis of Tudor-sn demonstrated that SN2 is the key domain required for the aggregation of Tudor-sn in SGs.