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Journal of Bacteriology, April 2005, p. 2908-2911, Vol. 187, No. 8
0021-9193/05/$08.00+0     doi:10.1128/JB.187.8.2908-2911.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

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

Susan Sharma,1 Johnny A. Davis,1,{dagger} Tulin Ayvaz,1 Beth Traxler,2 and Amy L. Davidson1*

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.

* Corresponding author. Mailing address: Department of Molecular Virology and Microbiology, Baylor College of Medicine, MS:BCM-280, One Baylor Plaza, Houston, TX 77030. Phone: (713) 798-4552. Fax: (713) 798-7375. E-mail: davidson{at}bcm.tmc.edu.

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

Journal of Bacteriology, April 2005, p. 2908-2911, Vol. 187, No. 8
0021-9193/05/$08.00+0     doi:10.1128/JB.187.8.2908-2911.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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