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Fig. 6. Vls physically interacts with Tud. (A) The eight Tudor (1-8) and two Tudor-like domains (1'-2') are depicted as purple boxes. Fragments of Tud (Golumbeski et al., 1991) used in pull-down assays are indicated below the map. N-and C-terminal amino acid residues of each fragment are indicated. (B) Western blot analysis of in vitro produced S•Tag-Tud fragments detected by using alkaline phosphatase-conjugated S proteins. (C) After incubation with GST or GST-Vsl, the bound Tud fragments were detected by immunoblotting using alkaline phosphatase-conjugated S proteins: the Tud-9A1-N and Tud-9A1-C fragments display a strong binding to GST-Vls, whereas Tud-JOZ and Tud-3ZS+L bind only weakly to it. GST alone (negative control) exhibits no binding to Tud-JOZ and Tud-9A1. Lower panels: input GST-Vls and GST proteins separated on a SDS-PAGE gel and stained with Coomassie.





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