Characterization of the dystrophin-syntrophin interaction using the two-hybrid system in yeast

FEBS Lett. 1996 Mar 25;383(1-2):124-8. doi: 10.1016/0014-5793(96)00214-1.

Abstract

The carboxy-terminal region of dystrophin has previously been shown to interact directly with alpha1 syntrophin, a cytoplasmic component of the dystrophin-glycoprotein complex, by in vitro biochemical studies such as overlay assay or immunoprecipitation. Using the two-hybrid system, we have isolated from a human heart cDNA library the entire coding sequence of human alpha1 syntrophin, therefore confirming for the first time this interaction via an in vivo approach. In addition, we have reduced the interaction domain to the distal half of alpha1 syntrophin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • Calcium-Binding Proteins
  • Cloning, Molecular
  • Conserved Sequence
  • DNA Primers
  • Dystrophin / chemistry
  • Dystrophin / metabolism*
  • Escherichia coli / genetics
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Muscle Proteins / chemistry
  • Muscle Proteins / genetics
  • Muscle Proteins / metabolism*
  • Myocardium / chemistry
  • Protein Binding
  • Saccharomyces cerevisiae / genetics
  • Sequence Alignment
  • Sequence Analysis
  • Transformation, Genetic / genetics

Substances

  • Calcium-Binding Proteins
  • DNA Primers
  • Dystrophin
  • Membrane Proteins
  • Muscle Proteins
  • syntrophin alpha1

Associated data

  • GENBANK/S81737