title: Characterization of Tudor-sn-containing granules in the silkworm, Bombyx mori.
abstract: 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.
authors: Laboratory of Silkworm Science, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences, Hakozaki 6-10-1, Fukuoka 812-8581, Japan.
authors: Li
authors: L
authors: Zhu
authors: Tsuneyuki
authors: T
authors: Tatsuke
authors: Hiroaki
authors: H
authors: Mon
authors: Zhiqing
authors: Z
authors: Li
authors: Jian
authors: J
authors: Xu
authors: Jae Man
authors: JM
authors: Lee
authors: Takahiro
authors: T
authors: Kusakabe
mesh_terms: D000818:Animals; D012831:Bombyx / Q000378:metabolism*; D055785:Gene Knockdown Techniques; D006358:Hot Temperature; D019476:Insect Proteins / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D013312:Stress, Physiological
chemical_list: D019476:Insect Proteins
keywords: Argonaute; BmN4 cells; Silkworm; Stress granules; Tudor-sn