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A Zn(II)-translocating P-type ATPase from Proteus mirabilis

C Rensing1, B Mitra, B P Rosen

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

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
|June 3, 1999
PubMed

Insights

Researchers identified a Proteus mirabilis gene complementing an Escherichia coli mutant lacking the ZntA zinc transporter. This P. mirabilis gene encodes a zinc-translocating P-type ATPase, crucial for heavy metal transport.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • A Proteus mirabilis mutant defective in swarming was previously isolated.
  • The mutation was mapped to a gene homologous to Escherichia coli zntA, which encodes a zinc-translocating P-type ATPase.

Purpose of the Study:

  • To characterize the function of the P. mirabilis gene homologous to E. coli zntA.
  • To confirm if the P. mirabilis gene encodes a functional zinc transporter.

Main Methods:

  • Complementation of an E. coli zntA-disrupted mutant with the P. mirabilis gene.
  • Assessing the P. mirabilis gene's ability to restore resistance to zinc and cadmium salts.
  • Measuring ATP-driven 65Zn(II) uptake in everted membrane vesicles from E. coli strains.

Main Results:

  • The P. mirabilis gene successfully complemented the zinc and cadmium sensitivity of the E. coli zntA mutant.
  • Everted membrane vesicles from the zntA-disrupted E. coli strain showed a loss of ATP-driven 65Zn(II) uptake.
  • Membrane vesicles from the complemented strain exhibited restored 65Zn(II) transport.

Conclusions:

  • The P. mirabilis homologue of E. coli ZntA is a functional Zn(II)-translocating P-type ATPase.
  • This P-type ATPase plays a role in heavy metal ion transport in P. mirabilis.

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