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N-terminal helicase domain, but not C-terminal dsRBD, of Dicer-2 is crucial for interaction with R2D2. HA-tagged transgenic Dicer-2 proteins in ovary lysate were immunoprecipitated by anti-HA beads and the copurified proteins were examined by Western blotting. αTubulin and Vasa served as loading controls and were not coimmunoprecipitated with HA-Dicer-2 proteins. The results were reproduced with three biologically replicated samples and representative images are shown.
