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Characterization of Tudor-sn-containing granules in the silkworm, Bombyx mori.
|Title||Characterization of Tudor-sn-containing granules in the silkworm, Bombyx mori.|
|Publication Type||Journal Article|
|Year of Publication||2013|
|Authors||Zhu L, Tatsuke T, Mon H, Li Z, Xu J, Lee JM, Kusakabe T|
|Journal||Insect biochemistry and molecular biology|
|Date Published||2013 Aug|
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.
|Alternate Journal||Insect Biochem. Mol. Biol.|