Arginine operator binding by heterologous and chimeric ArgR repressors from Escherichia coli and Bacillus stearothermophilus.

@article{Ghochikyan2002ArginineOB,
  title={Arginine operator binding by heterologous and chimeric ArgR repressors from Escherichia coli and Bacillus stearothermophilus.},
  author={Anahit Ghochikyan and Iovka Miltcheva Karaivanova and Mich{\`e}le Françoise Lecocq and Patricia Vusio and M P Arnaud and Marina Snapyan and Pierre Weigel and Laetitia Gu{\'e}vel and Malcolm Buckle and Vehary Sakanyan},
  journal={Journal of bacteriology},
  year={2002},
  volume={184 23},
  pages={6602-14}
}
Bacillus stearothermophilus ArgR binds efficiently to the Escherichia coli carAB operator, whereas the E. coli repressor binds very poorly to the argCo operator of B. stearothermophilus. In order to elucidate this contradictory behavior between ArgRs, we constructed chimeric proteins by swapping N-terminal DNA-binding and C-terminal oligomerization domains or by exchanging the linker peptide. Chimeras carrying the E. coli DNA-binding domain and the B. stearothermophilus oligomerization domain… CONTINUE READING

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