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    Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14326-31.

    The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase.

    Rensing C, Mitra B, Rosen BP.

    Source

    Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, 540 East Canfield Avenue, Detroit, MI 48201, USA.

    Abstract

    The first Zn(II)-translocating P-type ATPase has been identified as the product of o732, a potential gene identified in the sequencing of the Escherichia coli genome. This gene, termed zntA, was disrupted by insertion of a kanamycin gene through homologous recombination. The mutant strain exhibited hypersensitivity to zinc and cadmium salts but not salts of other metals, suggesting a role in zinc homeostasis in E. coli. Everted membrane vesicles from a wild-type strain accumulated 65Zn(II) and 109Cd(II) by using ATP as an energy source. Transport was sensitive to vanadate, an inhibitor of P-type ATPases. Membrane vesicles from the zntA::kan strain did not accumulate those metal ions. Both the sensitive phenotype and transport defect of the mutant were complemented by expression of zntA on a plasmid.

    PMID:
    9405611
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC24962
    Free PMC Article

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