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J. Biol. Chem., Vol. 279, Issue 31, 32116-32124, July 30, 2004

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AcrA, AcrB, and TolC of Escherichia coli Form a Stable Intermembrane Multidrug Efflux Complex^*

Elena B. Tikhonova and Helen I. Zgurskaya

From the Department of Chemistry and Biochemistry, the University of Oklahoma, Norman, Oklahoma 73019

Many transporters of Gram-negative bacteria involved in the extracellular secretion of proteins and the efflux of toxic molecules operate by forming intermembrane complexes. These complexes are proposed to span both inner and outer membranes and create a bridge across the periplasm. In this study, we analyzed interactions between the inner and outer membrane components of the tri-partite multidrug efflux pump AcrAB-TolC from Escherichia coli. We found that, once assembled, the intermembrane AcrAB-TolC complex is stable during the separation of the inner and outer membranes and subsequent purification. All three components of the complex co-purify when the affinity tag is attached to either of the proteins suggesting bi-partite interactions between AcrA, AcrB, and TolC. We show that antibiotics, the substrates of AcrAB-TolC, stabilize interactions within the complex. However, the formation of the AcrAB-TolC complex does not require an input of energy.

Received for publication, February 27, 2004 , and in revised form, May 13, 2004.

^* This study was supported by the National Institutes of Health Grant 1-RO1-AI052293-01A1. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Chemistry and Biochemistry, the University of Oklahoma, 620 Parrington Oval, Rm. 208, Norman, OK 73019. Tel.: 405-325-1678; Fax: 405-325-6111; E-mail: elenaz{at}ou.edu.

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