Molecular characterization of an anion pump. The arsA gene product is an arsenite(antimonate)-stimulated ATPase.

@article{Rosen1988MolecularCO,
  title={Molecular characterization of an anion pump. The arsA gene product is an arsenite(antimonate)-stimulated ATPase.},
  author={Barry P. Rosen and U. M. Weigel and Cyrus E Karkaria and Preeti Gangola},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 7},
  pages={
          3067-70
        }
}
The products of the arsenical resistance operon of resistance plasmid R733 form an efflux system for arsenicals. Detoxification results from active efflux of the oxyanions, preventing their concentration from reaching toxic levels. The largest polypeptide encoded by the ars operon was purified. From N-terminal sequencing the purified protein, termed the ArsA protein, was shown to correspond to the product of the arsA gene. The purified protein was demonstrated to bind ATP by two methods. First… CONTINUE READING
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