Figure 8From: Analysis of Thisbe and Pyramus functional domains reveals evidence for cleavage of Drosophila FGFsCleavage of Ths can be prevented through deletion of internal amino acids. (A) Thisbe amino acid sequence deleted in ThsΔ261-333Myc, including 5 potential cleavage sites, underlined in red; below the dotted black line are the amino acids that differ between the two deletion constructs, ThsΔ261-333Myc and ThsΔ261-356Myc, including 1 additional potential cleavage site, underlined in red. (B) Western blot of anti-HA immunoprecipitations from supernatant of cells transfected with pUASt-empty, HA-Ths-Myc, HA-ThsΔ261-333Myc, and HA-ThsΔ261-356Myc. HA-Ths-Myc was loaded 5x less than the other samples to equalize the exposure while resolving the double-band at 35 kD. ThsΔ261-333Myc (lane 3) is still partially cleaved but has increased full-length protein and (lane 4) ThsΔ261-356Myc has less cleavage and more full-length product, as compared to HA-Ths-Myc (lane 2). (C) 69B-GAL4 driving ThsΔ261-356Myc results in more Eve-positive cells in every hemisegment, as compared to wild-type. (D) ZenKr GAL4 driving ThsΔ261-356Myc results in extra Eve-positive cells outside the source of expression. (E) Eve-positive cells counted in 11 hemisegments for 25 embryos and averaged as in Fig. 5. The gray box represents the source of expression supported by ZenKr-GAL4. As compared to HA-Ths-Myc, ThsΔ261-356Myc has a decreased gradient of functional output, resulting in a flatter profile.Back to article page