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J. Biol. Chem., Vol. 279, Issue 26, 27799-27806, June 25, 2004

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Membrane Topology of the DrrB Protein of the Doxorubicin Transporter of Streptomyces peucetius^*

Suvarna M. Gandlur, Ling Wei, Jeoffery Levine, Jack Russell, and Parjit Kaur

From the Department of Biology, Georgia State University, Atlanta, Georgia 30303

Daunorubicin and doxorubicin, two commonly used anticancer agents, are produced by the soil bacterium Streptomyces peucetius. Self-resistance to these antibiotics in S. peucetius is conferred by the drrAB locus that codes for two proteins, DrrA and DrrB. DrrA is an ATP-binding protein. It belongs to the ABC family of transporters and shares sequence and functional similarities with P-glycoprotein of cancer cells. DrrB is an integral membrane protein that might function as a transporter for the efflux of daunorubicin and doxorubicin. Together, DrrA and DrrB are believed to form an ATP-driven pump for the efflux of these drugs. The drrAB locus has been cloned, and the two proteins have been expressed in a functional form in Escherichia coli. A topological analysis of the DrrB protein was performed using gene fusion methodology. Random and site-directed fusions of the drrB gene to lacZ, phoA, or gfp reporter genes were created. Based on the fusion data, a topological model of the DrrB protein is proposed in which the protein has eight membrane-spanning domains with both the N terminus and the C terminus in the cytoplasm.

Received for publication, March 15, 2004 , and in revised form, April 16, 2004.

^* 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. Tel.: 404-651-3864; Fax: 404-651-2509; E-mail: pkaur{at}gsu.edu.

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