Abstract

R-factor mediated bacterial resistance to arsenical salts occurs by active extrusion of the toxic oxyanions from cells of gram negative bacteria. The ars operon of the conjugative plasmid R773 encodes an anion pump. The pump has two polypeptide components. The catalytic subunit, the ArsA protein, is an oxyanion-stimulated ATPase. The membrane component, the ArsB protein, has been localized in the inner membrane of Escherichia coli. The ArsA and ArsB proteins have been postulated to form a membrane complex which functions as an anion-translocating ATPase. In this study evidence is presented showing that expression of the arsB gene is required to anchor the ArsA protein to the inner membrane. Binding studies with purified ArsA to membranes with and without the arsB gene product confirm this requirement. Membranes of uncA mutants containing both the ArsA and ArsB proteins exhibit arsenite(antimonite)-stimulated ATPase activity. These results support the model in which the ArsA protein is the catalytic energy transducing component of the anion pump, whereas the integral membrane ArsB protein serves as both the anion channel and membrane binding site for the ArsA protein.

Department

Molecular, Cellular and Biomedical Sciences

Publication Date

1-5-1990

Journal Title

Journal of Biological Chemistry

Publisher

American Society for Biochemistry and Molecular Biology

Document Type

Article

Comments

This research was originally published in Journal of Biological Chemistry. Tisa, L.S. and B.P. Rosen. 1990. Molecular characterization of an anion pump. The ArsB protein is the membrane anchor to the ArsA protein. J. Biol. Chem. 265:190-194. © the American Society for Biochemistry and Molecular Biology. http://www.jbc.org/content/265/1/190.abstract

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