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. 1998 Jul 13;142(1):251–261. doi: 10.1083/jcb.142.1.251

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Qualitative and quantitative yeast two-hybrid analysis of the interaction between Drosophila ankyrin and neuroglian¹⁶⁷ cytoplasmic domains with tyrosine to phenylalanine amino acid substitutions. (A) Qualitative yeast two-hybrid analysis of the interaction between Y to F neuroglian cytoplasmic domain mutations and Drosophila ankyrin. Blue colonies result from the induction of β-galactosidase activity and indicate an interaction between the two GAL4 fusion proteins. Top row, yeast colonies containing a pACTII–Drosophila ankyrin construct (expressing a GAL4 activation domain–Drosophila ankyrin fusion protein) as well as a pAS1-CYH2 construct (expressing a fusion protein consisting of the GAL4 DNA-binding domain and a neuroglian cytoplasmic domain, which was either wild-type or contained one or two point mutations resulting in Y to F amino acid substitutions); bottom row, yeast colonies containing the same pAS1–CYH2 constructs and a pACTII vector control. (B) Quantitative evaluation of β-galactosidase expression in the yeast cells shown in A. Data bars represent the mean ± SD from two different experiments performed in triplicate determinations.

Qualitative and quantitative yeast two-hybrid analysis of the interaction between Drosophila ankyrin and neuroglian¹⁶⁷ cytoplasmic domains with tyrosine to phenylalanine amino acid substitutions. (A) Qualitative yeast two-hybrid analysis of the interaction between Y to F neuroglian cytoplasmic domain mutations and Drosophila ankyrin. Blue colonies result from the induction of β-galactosidase activity and indicate an interaction between the two GAL4 fusion proteins. Top row, yeast colonies containing a pACTII–Drosophila ankyrin construct (expressing a GAL4 activation domain–Drosophila ankyrin fusion protein) as well as a pAS1-CYH2 construct (expressing a fusion protein consisting of the GAL4 DNA-binding domain and a neuroglian cytoplasmic domain, which was either wild-type or contained one or two point mutations resulting in Y to F amino acid substitutions); bottom row, yeast colonies containing the same pAS1–CYH2 constructs and a pACTII vector control. (B) Quantitative evaluation of β-galactosidase expression in the yeast cells shown in A. Data bars represent the mean ± SD from two different experiments performed in triplicate determinations.