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Free Content The dimerization and topological specificity functions of MinE reside in a structurally autonomous C-terminal domain

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Correct placement of the division septum in Escherichia coli requires the co-ordinated action of three proteins, MinC, MinD and MinE. MinC and MinD interact to form a non-specific division inhibitor that blocks septation at all potential division sites. MinE is able to antagonize MinCD in a topologically sensitive manner, as it restricts MinCD activity to the unwanted division sites at the cell poles. Here, we show that the topological specificity function of MinE residues in a structurally autonomous, trypsin-resistant domain comprising residues 31–88. Nuclear magnetic resonance (NMR) and circular dichroic spectroscopy indicate that this domain includes both α and β secondary structure, while analytical ultracentrifugation reveals that it also contains a region responsible for MinE homodimerization. While trypsin digestion indicates that the anti-MinCD domain of MinE (residues 1–22) does not form a tightly folded structural domain, NMR analysis of a peptide corresponding to MinE1–22 indicates that this region forms a nascent helix in which the peptide rapidly interconverts between disordered (random coil) and α-helical conformations. This suggests that the N-terminal region of MinE may be poised to adopt an α-helical conformation when it interacts with the target of its anti-MinCD activity, presumably MinD.
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Document Type: Research Article

Affiliations: 1: Department of Biochemistry, University of Sydney, Sydney, NSW 2006, Australia., 2: Department of Microbiology, University of Connecticut Health Center, Farmington, CT 06030, USA., 3: Department of Biochemistry, University of Connecticut Health Center, Farmington, CT 06030, USA.

Publication date: February 1, 1999

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