Figure 3 | Scientific Reports

Figure 3

From: Germ plasm localisation of the HELICc of Vasa in Drosophila: analysis of domain sufficiency and amino acids critical for localisation

Figure 3

Localisation analysis of truncated Drosophila Vasa (DmVas) proteins, chimeric Vas proteins and helicase superfamily C-terminal domains (HELICc) from other animal species.

All Vas proteins were green fluorescent protein (GFP)-tagged and analyses were performed in egg chambers from Stages 9–13 of oogenesis. Each panel shows the posterior half of the oocyte. (A–A”’) GFP-DmVas460–661: sequence N-terminal to HELICc was truncated; (B–B”’) GFP-DmVas460–621/HELICc (abbreviated as DmVas460–621): a sole HELICc. Posterior localisation of DmVas460–661 and DmVas460–621/HELICc was detected; (C–C”’) GFP-DmVas1–460: a C-terminal truncated DmVas polypeptide without the HELICc and C-terminal sequences. (D–D”’) GFP-DmVas470–661: an N-terminal truncated DmVas polypeptide without the N-terminal sequence, DEXDc and 10 residues in the N-terminus of HELICc. Posterior localisation of DmVas1–460 and DmVas470–661 was not detected; (E–E”’) GFP-ApDHELICc: a ApVas1–DmVas chimeric protein in which the N-terminal sequence and most of the DEXDc domain sequences of DmVas were replaced by those from ApVas1. Posterior localisation was detected; (F–F”’ to I–I”’) GFP-tagged HELICc of Vas orthologs from the pea aphid (F–F”’, GFP-ApVas1HELICc), cricket (G–G”’, GFP-GbVasHELICc), grasshopper (H–H”’, GFP-SgVasHELICc) and mouse (I–I”’, GFP-MvhHELICc). Posterior localisation could be detected only in the egg chamber expressing SgVasHELICc (H–H”’). In all panels, anterior is to the left and posterior is to the right. Scale bars, 25 μm.

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