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

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.

SUBMITTER: Rensing C

PROVIDER: S-EPMC24962 | biostudies-literature | 1997 Dec

REPOSITORIES: biostudies-literature

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

Rensing C C Mitra B B Rosen B P BP

Proceedings of the National Academy of Sciences of the United States of America 19971201 26

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 1 ...[more]

PMID: 9405611

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