Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

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

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

PMC Copyright notice

A qualitative and quantitative yeast two-hybrid analysis maps the minimal ankyrin binding site to a 17-amino acid segment within the Drosophila neuroglian cytoplasmic domain with the next 19 carboxy-terminal amino acid residues being required for high efficiency binding. (A) Qualitative yeast two-hybrid analysis of the interaction between neuroglian cytoplasmic domain fragments 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 wild-type or deleted neuroglian cytoplasmic domain); bottom row, yeast colonies containing the same pAS1–CYH2 constructs and a pACTII vector control that did not result in an activation of β-galactosidase expression. (B) Quantitative analysis of the effects of neuroglian cytoplasmic deletions on the yeast two-hybrid neuroglian–ankyrin interaction. Data bars represent the mean ± SD from three different yeast colonies performed in triplicate determinations.

A qualitative and quantitative yeast two-hybrid analysis maps the minimal ankyrin binding site to a 17-amino acid segment within the Drosophila neuroglian cytoplasmic domain with the next 19 carboxy-terminal amino acid residues being required for high efficiency binding. (A) Qualitative yeast two-hybrid analysis of the interaction between neuroglian cytoplasmic domain fragments 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 wild-type or deleted neuroglian cytoplasmic domain); bottom row, yeast colonies containing the same pAS1–CYH2 constructs and a pACTII vector control that did not result in an activation of β-galactosidase expression. (B) Quantitative analysis of the effects of neuroglian cytoplasmic deletions on the yeast two-hybrid neuroglian–ankyrin interaction. Data bars represent the mean ± SD from three different yeast colonies performed in triplicate determinations.