Identification of the Escherichia coli K‐12 Nramp orthologue (MntH) as a selective divalent metal ion transporter

Molecular Microbiology - Tập 35 Số 5 - Trang 1065-1078 - 2000
Hortence Makui1, E A Roig1, Stewart T. Cole2, John D. Helmann3, Philippe Gros4, Mathieu Cellier1
1INRS-Institut Armand-Frappier, 531 Bd des prairies, Laval H7V 1B7, PQ, Canada.
2Unité de Génétique Moléculaire Bactérienne, Institut Pasteur, 25/28 rue du Docteur Roux, 75724 Paris Cedex 15, France
3Section of Microbiology, Wing Hall, Cornell University, Ithaca, NY 14853-8101, USA.
4Department of Biochemistry, McGill University, 3655 Drummond, Montréal H3G 1Y6, PQ, Canada.

Tóm tắt

The Escherichia coli mntH (formerly yfeP) gene encodes a putative membrane protein (MntH) highly similar to members of the eukaryotic Nramp family of divalent metal ion transporters. To determine the function of E. coli MntH, a null mutant was created and MntH was overexpressed both in wild‐type E. coli and in the metal‐dependent mutant hflB1(Ts). At the restrictive temperature 42°C, the mntH null mutation reduces the suppression of hflB1(Ts) thermosensitivity by exogenous divalent metals. Conversely, overexpression of MntH restores growth at 42°C, increases suppression of the ts phenotype by Fe(II) and Ni(II) and renders hflB1(Ts) cells hypersensitive to Mn(II). Transport studies in intact cells show that MntH selectively facilitates uptake of 54Mn(II) and 55Fe(II) in a temperature‐, time‐ and proton‐dependent manner. Competition studies in uptake assays and growth inhibition experiments in hflB1(Ts) mutants together indicate that MntH is a divalent metal cation transporter of broad substrate specificity. The functional characteristics of MntH suggest that it corresponds to the previously described manganese transporter of E. coli. This study indicates that proton‐dependent divalent metal ion uptake has been preserved in the Nramp family from bacteria to humans.

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Molecular Microbiology

Tập 35 Số 5

1065-1078

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