In vitro selection by using mutated GCN4-bZIP peptides for analysis of peptide-DNA interactions

Nucleic Acids Symp Ser. 2000:(44):245-6. doi: 10.1093/nass/44.1.245.

Abstract

In vitro selection has been used as a method to determine the optimal binding site for DNA-binding proteins. We report here in vitro selection of dsDNA sequences that bind to mutated-GCN4-bZIP peptides. The GCN4-bZIP peptide mutated from alanine to histidine on a position-14 that contacts with DNA bound to different sequence from a binding site of wild type peptide.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Basic-Leucine Zipper Transcription Factors
  • Binding Sites / genetics
  • DNA / chemistry
  • DNA / genetics
  • DNA / metabolism*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics*
  • DNA-Binding Proteins / metabolism*
  • G-Box Binding Factors
  • In Vitro Techniques
  • Kinetics
  • Mutagenesis
  • Protein Binding
  • Protein Kinases / chemistry
  • Protein Kinases / genetics*
  • Protein Kinases / metabolism*
  • Quartz
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / genetics*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Selection, Genetic
  • Transcription Factors / chemistry
  • Transcription Factors / genetics*
  • Transcription Factors / metabolism*

Substances

  • Basic-Leucine Zipper Transcription Factors
  • DNA-Binding Proteins
  • G-Box Binding Factors
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Quartz
  • DNA
  • Protein Kinases