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PMID: 7766211 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Ion efflux systems involved in bacterial metal resistances.

Journal of industrial microbiology ·Vol. 14 ·No. 2 ·1995-02-00 ·Pages 186-99

Nies DH, Silver S

Abstract

Studying metal ion resistance gives us important insights into environmental processes and provides an understanding of basic living processes. This review concentrates on bacterial efflux systems for inorganic metal cations and anions, which have generally been found as resistance systems from bacteria isolated from metal-polluted environments. The protein products of the genes involved are sometimes prototypes of new families of proteins or of important new branches of known families. Sometimes, a group of related proteins (and presumedly the underlying physiological function) has still to be defined. For example, the efflux of the inorganic metal anion arsenite is mediated by a membrane protein which functions alone in Gram-positive bacteria, but which requires an additional ATPase subunit in some Gram-negative bacteria. Resistance to Cd2+ and Zn2+ in Gram-positive bacteria is the result of a P-type efflux ATPase which is related to the copper transport P-type ATPases of bacteria and humans (defective in the human hereditary diseases Menkes' syndrome and Wilson's disease). In contrast, resistance to Zn2+, Ni2+, Co2+ and Cd2+ in Gram-negative bacteria is based on the action of proton-cation antiporters, members of a newly-recognized protein family that has been implicated in diverse functions such as metal resistance/nodulation of legumes/cell division (therefore, the family is called RND). Another new protein family, named CDF for 'cation diffusion facilitator' has as prototype the protein CzcD, which is a regulatory component of a cobalt-zinc-cadmium resistance determinant in the Gram-negative bacterium Alcaligenes eutrophus. A family for the ChrA chromate resistance system in Gram-negative bacteria has still to be defined.

Related Genes
MeSH Terms
ATP-Binding Cassette Transporters/physiology Adenosine Triphosphatases/physiology Alcaligenes/genetics,metabolism Bacteria/genetics,metabolism Drug Resistance, Microbial/genetics,physiology Escherichia coli/genetics,metabolism Ion Transport/genetics,physiology Metals/pharmacokinetics Staphylococcus/genetics,metabolism
Chemicals
ATP-Binding Cassette Transporters Metals Adenosine Triphosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Nies D H
Institut für Mikrobiologie, Martin-Luther-Universität, Halle, Germany.
Silver S
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Article Info
Journal
Journal of industrial microbiology
Abbr.
J Ind Microbiol
ISSN
0169-4146
Published
1995-02-00
Pages
186-99
Language
English
Region
England
NLM ID
8610887
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