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Related Experiment Videos

Complementation between nucleotide binding domains in an anion-translocating ATPase

P Kaur1, B P Rosen

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

Journal of Bacteriology
|January 1, 1993
PubMed
Summary
This summary is machine-generated.

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The ArsA protein

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • The plasmid-encoded ars operon in Escherichia coli confers arsenical resistance.
  • The ArsA protein is the catalytic component of this arsenical-translocating ATPase.
  • ArsA is a homodimer with two nucleotide-binding domains (A1 and A2) per subunit.

Purpose of the Study:

  • To investigate the functional requirement of the two nucleotide-binding domains (A1 and A2) within the ArsA protein.
  • To determine if the A1 and A2 domains must be present in a single polypeptide for arsenical resistance.
  • To elucidate the catalytic mechanism of the ArsA ATPase.

Main Methods:

  • Subcloning of the arsA gene into two halves (arsA1 and arsA2) and expression in compatible plasmids.

Related Experiment Videos

  • Assessing arsenical resistance in E. coli cells coexpressing arsA1 and arsA2.
  • Employing genetic complementation studies with subclones and point mutations in arsA1 and arsA2.

    • Main Results:

    • Neither the arsA1 nor arsA2 half-gene alone conferred arsenical resistance.
    • Coexpression of arsA1 and arsA2 in trans resulted in arsenical resistance.
    • Genetic complementation confirmed that a functional ArsA requires both A1 and A2 domains, which can be supplied in trans.

    Conclusions:

    • The ArsA protein's catalytic activity and arsenical resistance function require both A1 and A2 nucleotide-binding domains.
    • These domains do not need to be on the same polypeptide chain; they can function in a trans-complemented manner.
    • A model is proposed where the ArsA dimer forms two catalytic units, each comprising an A1 domain from one monomer and an A2 domain from the other.