Hyperthermophilic Thermotoga arginine repressor binding to full-length cognate and heterologous arginine operators and to half-site targets.

@article{Morin2003HyperthermophilicTA,
  title={Hyperthermophilic Thermotoga arginine repressor binding to full-length cognate and heterologous arginine operators and to half-site targets.},
  author={Andr{\'e}J. Morin and Nadine Huysveld and Fr{\'e}d{\'e}rique Braun and Diliana Dimova and Vehary Sakanyan and Daniel Charlier},
  journal={Journal of molecular biology},
  year={2003},
  volume={332 3},
  pages={
          537-53
        }
}
The degree of sequence conservation of arginine repressor proteins (ArgR) and of the cognate operators (tandem pairs of 18 bp imperfect palindromes, ARG boxes) in evolutionarily distant bacteria is unusually high, and the global mechanism of ArgR-mediated regulation appears to be similar. However, here we demonstrate that the arginine repressor from the hyperthermophilic bacterium Thermotoga neapolitana (ArgR(Tn)) exhibits characteristics that clearly distinguish this regulator from the well… CONTINUE READING

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