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Pb(II)-translocating P-type ATPases

C Rensing1, Y Sun, B Mitra

  • 1Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan 48201, USA.

The Journal of Biological Chemistry
|November 26, 1998
PubMed
Summary
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Staphylococcus aureus CadA and Escherichia coli ZntA are identified as lead(II) pumps, not just cadmium pumps. This finding expands our understanding of metal ion transport mechanisms in bacteria.

Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • The cad operon in Staphylococcus aureus confers cadmium resistance via CadA, an ATP-coupled Cd(II) pump.
  • Escherichia coli possesses a homologue, ZntA, also known as a Zn(II)/Cd(II) pump.
  • CadC acts as a metal-responsive repressor within the cad operon.

Purpose of the Study:

  • To investigate the potential of CadA and ZntA as lead(II) pumps.
  • To characterize the metal specificity of the CadC repressor.

Main Methods:

  • Assessing metal resistance conferred by CadA and ZntA.
  • Evaluating the effect of lead(II) on zinc(II) transport mediated by CadA and ZntA in everted membrane vesicles.
  • Determining the metal response profile of the CadC repressor.

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Main Results:

  • CadC exhibits a metal response order of Pb(II) > Cd(II) > Zn(II).
  • Both CadA and ZntA confer resistance to lead(II).
  • Lead(II) inhibits the transport of zinc(II) catalyzed by CadA and ZntA.

Conclusions:

  • CadA and ZntA function as lead(II) pumps, expanding their known substrate range.
  • The CadC repressor's specificity suggests a broader role in regulating resistance to multiple soft metals.
  • These findings have implications for understanding bacterial metal homeostasis and resistance mechanisms.