Figure 11.

E. multilocularis insulin-like peptides and yeast two-hybrid experiments. A) Amino acid sequence comparison between the E. multilocularis insulin-like peptides EmILP1 and EmILP2 and human insulin (Hins). Highly conserved residues are printed in white on black background, residues with similar biochemical features are printed in black on grey background. Underlined sequences indicate predicted signal peptides. Asterisks indicate cysteine residues important for disulphide-bridge formation. B) Yeast two-hybrid experiments. Translational fusions were generated for the Gal4 activation domain (Gal4-AD) and the LBDs of the human insulin receptor (HIR-LBD) as well as the E. multilocularis receptors EmIR1 (EmIR1-LBD) and EmIR2 (EmIR2-LBD). The Gal4 DNA binding domain (Gal4-BD) was fused to human pro-insulin (H pro-ins) as well as to EmILP1 and EmILP2. Yeast strains were double transformed with the plasmid constructs as indicated and growth under different stringency conditions [10] was assessed. ‘-‘ indicates no growth, ‘++’ growth under medium stringency conditions, ‘+++’ growth under high stringency conditions. LBDs, ligand binding domains.

Hemer et al. BMC Biology 2014 12:5   doi:10.1186/1741-7007-12-5
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