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A plasmid-encoded anion-translocating ATPase.

B P Rosen1, C M Hsu, C E Karkaria

  • 1Department of Biochemistry, Wayne State University, School of Medicine, Detroit, MI 48201.

Biochimica Et Biophysica Acta
|July 25, 1990
PubMed
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An ATP-driven oxyanion pump, encoded by the arsenical resistance operon, extrudes toxic oxyanions like arsenite and arsenate. This mechanism confers resistance by maintaining low intracellular oxyanion concentrations.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Arsenical compounds pose significant toxicity threats.
  • Resistance mechanisms in bacteria are crucial for understanding microbial survival and developing antimicrobial strategies.
  • The arsenical resistance operon (ars) in plasmid R773 confers resistance to toxic oxyanions.

Purpose of the Study:

  • To identify and characterize the molecular components responsible for arsenical resistance.
  • To elucidate the function of the anion-translocating ATPase in oxyanion extrusion.
  • To understand the genetic basis of substrate specificity in the arsenical resistance pump.

Main Methods:

  • Expression of the arsenical resistance operon in Escherichia coli.
  • Biochemical assays to determine ATPase activity and substrate specificity.

Related Experiment Videos

  • Genetic analysis of arsA, arsB, and arsC genes.

    • Main Results:

    • The arsenical resistance operon encodes an ATP-driven anion pump.
    • The pump, composed of ArsA and ArsB proteins, extrudes arsenite and antimonite.
    • The ArsC protein expands the pump's activity to include arsenate extrusion, conferring resistance to all three oxyanions.

    Conclusions:

    • The identified anion-translocating ATPase is a key component of the arsenical resistance system.
    • The ArsA/ArsB complex functions as an oxyanion pump, while ArsC broadens its substrate range.
    • Understanding this resistance mechanism provides insights into cellular detoxification processes and potential therapeutic targets.