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Volume 272, Number 1, Issue of January 3, 1997 pp. 326-331
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Alternate Energy Coupling of ArsB, the Membrane Subunit of the Ars Anion-translocating ATPase

(Received for publication, August 26, 1996, and in revised form, October 9, 1996)

From the Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan 48201

The arsenical resistance (ars) operon of the conjugative R-factor R773 confers resistance to arsenical and antimonial compounds in Escherichia coli, where resistance results from active extrusion of arsenite catalyzed by the products of the arsA and arsB genes. Previous in vivo studies on the energetics of arsenite extrusion showed that expression of both genes produced an ATP-coupled arsenite extrusion system that was independent of the electrochemical proton gradient. In contrast, in cells expressing only the arsB gene, arsenite extrusion was coupled to electrochemical energy and independent of ATP, suggesting that the Ars transport system exhibits a dual mode of energy coupling depending on the subunit composition. In vitro the ArsA-ArsB complex has been shown to catalyze ATP-coupled uptake of ⁷³AsO₂¹ in everted membrane vesicles. However, transport catalyzed by ArsB alone has not previously been observed in vitro. In this study we demonstrate everted membrane vesicles prepared from cells expressing only arsB exhibit uptake of ⁷³AsO₂¹ coupled to electrochemical energy.

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