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Mol Microbiol. 1998 Oct;30(2):265-73.

The relationship between hetero-oligomer formation and function of the topological specificity domain of the Escherichia coli MinE protein.

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Department of Microbiology, University of Connecticut Health Center, Farmington, CT 06032, USA.


MinE is an oligomeric protein that, in conjunction with other Min proteins, is required for the proper placement of the cell division site of Escherichia coli. We have examined the self-association properties of MinE by analytical ultracentrifugation and by studies of hetero-oligomer formation in non-denaturing polyacrylamide gels. The self-association properties of purified MinE predict that cytoplasmic MinE is likely to exist as a mixture of monomers and dimers. Consistent with this prediction, the C-terminal MinE22-88 fragment forms hetero-oligomers with MinE+ when the proteins are co-expressed. In contrast, the MinE36-88 fragment does not form MinE+/MinE36-88 hetero-oligomers, although MinE36-88 affects the topological specificity of septum placement as shown by its ability to induce minicell formation when co-expressed with MinE+ in wild-type cells. Therefore, hetero-oligomer formation is not necessary for the induction of minicelling by expression of MinE36-88 in wild-type cells. The interference with normal septal placement is ascribed to competition between MinE36-88 and the corresponding domain in the complete MinE protein for a component required for the topological specificity of septal placement.

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