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Journal of Bacteriology, February 2000, p. 613-619, Vol. 182, No. 3
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Membrane Redistribution of the Escherichia coli MinD Protein Induced by MinE

S. L. Rowland, X. Fu, M. A. Sayed, Y. Zhang, W. R. Cook, and L. I. Rothfield^*

Department of Microbiology, University of Connecticut Health Center, Farmington, Connecticut 06032

Received 26 April 1999/Accepted 3 November 1999

Escherichia coli cells contain potential division sites at midcell and adjacent to the cell poles. Selection of the correct division site at midcell is controlled by three proteins: MinC, MinD, and MinE. It has previously been shown (D. Raskin and P. de Boer, Cell 91:685-694, 1997) that MinE-Gfp localizes to the midcell site in an MinD-dependent manner. We use here Gfp-MinD to show that MinD associates with the membrane around the entire periphery of the cell in the absence of the other Min proteins and that MinE is capable of altering the membrane distribution pattern of Gfp-MinD. Studies with the isolated N-terminal and C-terminal MinE domains indicated different roles for the two MinE domains in the redistribution of membrane-associated MinD.

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^* Corresponding author. Mailing address: Department of Microbiology, University of Connecticut Health Center, Farmington, CT 06032. Phone: (860) 679-3581. Fax: (860) 679-1239. E-mail: lroth{at}panda.uchc.edu.

Present address: Department of Biochemistry, UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ 08854.

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Journal of Bacteriology, February 2000, p. 613-619, Vol. 182, No. 3
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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