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J Biol Chem, Vol. 274, Issue 37, 26065-26070, September 10, 1999
From the Institut für Mikrobiologie, Kurt-Mothes-Str. 3, D-06099 Halle, Germany
The membrane-bound CzcA protein, a member of the
resistance-nodulation-cell division (RND) permease superfamily, is part
of the CzcCB2A complex that mediates heavy metal
resistance in Ralstonia sp. CH34 by an active cation efflux
mechanism driven by cation/proton antiport. CzcA was purified to
homogeneity after expression in Escherichia coli,
reconstituted into proteoliposomes, and the kinetics of heavy metal
transport by CzcA was determined. CzcA is composed of 12 transmembrane
Energetics and Topology of CzcA, a Cation/Proton Antiporter of
the Resistance-Nodulation-Cell Division Protein Family
-helices and two large periplasmic domains. Two conserved aspartate
and a glutamate residue in one of these transmembrane spans are
essential for heavy metal resistance and proton/cation antiport but not
for facilitated diffusion of cations. Generalization of the resulting
model for the function of CzcA as a two-channel pump might help to
explain the functions of other RND proteins in bacteria and eukaryotes.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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