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Functional Reassembly of the Escherichia coli Maltose Transporter following Purification of a MalF-MalG Subassembly

Susan Sharma,¹ Johnny A. Davis,^1, Tulin Ayvaz,¹ Beth Traxler,² and Amy L. Davidson^1*

Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas,¹ Department of Microbiology, University of Washington, Seattle, Washington²

Received 27 May 2004/ Accepted 5 January 2005

Taking advantage of a chaperone-like function of MalK, a stable complex of MalF-MalG could be solubilized from the Escherichia coli membrane and purified in high yield in the absence of MalK. This MalF-MalG complex was competent for efficient reassembly of a functional MalFGK₂ maltose transporter complex both in detergent solution and in proteoliposomes.

Present address: Department of Microbiology and Cell Science, University of Florida, Gainesville, FL 32611.

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