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Journal of Bacteriology, November 2001, p. 6684-6687, Vol. 183, No. 22
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.22.6684-6687.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

The Dimerization Function of MinC Resides in a Structurally Autonomous C-Terminal Domain

Tim H. Szeto, Susan L. Rowland, and Glenn F. King*

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

Received 27 April 2001/Accepted 13 August 2001

Limited proteolysis of the Escherichia coli cell division inhibitor MinC reveals that its dimerization function resides in a structurally autonomous C-terminal domain. We show that cytoplasmic MinC is poised near the monomer-dimer equilibrium and propose that it only becomes entirely dimeric once recruited to the membrane by MinD.

* Corresponding author. Mailing address: Department of Biochemistry, MC3305, University of Connecticut Health Center, 263 Farmington Ave., Farmington, CT 06032. Phone: (860) 679-8364. Fax: (860) 679-1652. E-mail: glenn{at}psel.uchc.edu.

Journal of Bacteriology, November 2001, p. 6684-6687, Vol. 183, No. 22
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.22.6684-6687.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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