Characterization of the dimerization domain in the FNR transcription factor.

@article{Moore2001CharacterizationOT,
  title={Characterization of the dimerization domain in the FNR transcription factor.},
  author={Laura Jane Moore and Patricia Kiley},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 49},
  pages={45744-50}
}
The global anaerobic regulator FNR from Escherichia coli is a dimeric Fe-S protein that is inactivated by O(2) through disruption of its [4Fe-4S] cluster and conversion to a monomeric form. As a first step in elucidating the molecular interactions that control FNR dimerization, we have performed alanine-scanning mutagenesis of a potential dimerization domain. Replacement of many hydrophobic residues (Met-143, Met-144, Leu-146, Met-147, Ile-151, Met-157, and Ile-158) and two charged residues… CONTINUE READING