Characterization of Tudor-sn-containing granules in the silkworm,Bombyx mori |
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| Authors: | Li Zhu Tsuneyuki Tatsuke Hiroaki Mon Zhiqing Li Jian Xu Jae Man Lee Takahiro Kusakabe |
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| Institution: | 1. Laboratory of Microbiology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 111-0033, Japan;2. Transgenic Silkworm Research Unit, National Institute of Agrobiological Sciences, 1-2 Owashi, Tsukuba, Ibaraki 305-8634, Japan;1. Department of Microbiology & Immunology, University of California San Francisco, San Francisco, CA 94143, USA;2. Sandler Asthma Basic Research Center, University of California San Francisco, San Francisco, CA 94143, USA;3. Department of Cell & Tissue Biology, University of California San Francisco, San Francisco, CA 94143, USA;1. Jiangsu Key Laboratory for Biodiversity and Biotechnology, College of Life Sciences, Nanjing Normal University, Nanjing 210023, P.R. China;1. Department of Biotechnology, Tokyo University of Agriculture and Technology, 2-24-16 Naka-chou, Koganei, Tokyo 184-8588, Japan;2. School of Dentistry at Matsudo, Nihon University, 2-870-1 Sakaecho-nishi, Matsudo, Chiba 271-8587, Japan |
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| 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. |
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| Keywords: | Stress granules BmN4 cells Silkworm Argonaute Tudor-sn |
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