Site-directed mutagenesis of the A-factor receptor protein: Val-41 important for DNA-binding and Trp-119 important for ligand-binding.

@article{Sugiyama1998SitedirectedMO,
  title={Site-directed mutagenesis of the A-factor receptor protein: Val-41 important for DNA-binding and Trp-119 important for ligand-binding.},
  author={Masakazu Sugiyama and Hiroyasu Onaka and Tsuyoshi Nakagawa and Sueharu Horinouchi},
  journal={Gene},
  year={1998},
  volume={222 1},
  pages={133-44}
}
The A-factor receptor protein (ArpA) plays a key role in the regulation of secondary metabolism and cellular differentiation in Streptomyces griseus. ArpA binds the target DNA site forming a 22 bp palindrome in the absence of A-factor, and exogenous addition of A-factor to the ArpA-DNA complex immediately releases ArpA from the DNA. An amino acid (aa) replacement at Val-41 to Ala in an alpha-helix-turn-alpha-helix (HTH) motif at the N-terminal portion of ArpA abolished DNA-binding activity but… CONTINUE READING

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