Changing the binding specificity of a repressor by redesigning an alpha-helix.
We replaced amino acids on the 'outside', or solvent-exposed, surface of the DNA recognition alpha-helix of 434 repressor with the corresponding amino acids from the recognition helix of P22 repressor. The binding specificity of the resulting hybrid protein, as measured in vivo and in vitro, was that of P22 repressor.
D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000235:genetics*; D004279:DNA, Viral / Q000235:genetics; D009876:Operon; D011487:Protein Conformation; D012097:Repressor Proteins; D014157:Transcription Factors
D004279:DNA, Viral; D012097:Repressor Proteins; D014157:Transcription Factors