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Fig. 2. dVps16A and dVps16B bind different Vps33 homologs. (A) The domain of highest similarity between the two Vps16 homologs in the Drosophila genome is the Vps16-C domain [Pfam04840 in the Conserved Domain Database (Marchler-Bauer et al., 2005)]. (B) Sequences of Vps16 proteins were aligned using ClustalW and a phylogenetic tree was constructed using 1000 bootstraps. Accession numbers: Tetraodon nigroviridis Vps16B (TnVps16: CAF92974, zebrafish Vps16B (DrVps16B: AAQ945721), human Vps16s (Hsvps16A: AAG346781 and HsVps16B: AAD096241) and mouse Vps16s (MmVps16A: AAH256261 and MmVps16B: BAC326801), Anopheles gambia (AgVps16A: XP_310557.1 and AgVps16B: XP_321923.1), Drosophila melanogaster (DmVps16A: NP_649877.1 and DmVps16B: AAF569461) Drosophila pseudoobscura (DpVps16B: EAL281241), Arabidopsis thaliana VACUOLELESS1 (AtVps16: AAM981051) and Saccharomyces cervisiae Vps16p (ScVps16p: NP_015280.1). (C) Myc-tagged Rop, dVps33B or Car proteins were co-expressed in S2 cells with HA-tagged dVsp16A and detected in input samples by immunoblots (IB) with anti-dVps16A or anti-Myc antibodies. Proteins were immunoprecipitated with anti-dVps16A antibodies. Immunoprecipitated proteins (IP) were detected with anti-Myc antibodies. (D) HA-tagged Rop, dVps33B or Car proteins were co-expressed in S2 cells with a Myc-tagged dVsp16A and detected in input samples by immunoblots (IB) with anti-HA or anti-Myc antibodies. Proteins were immunoprecipitated with anti-Myc antibodies. Immunoprecipitated proteins (IP) were detected with anti-HA antibodies.
