PMID:10096083
| Citation |
King, GF, Rowland, SL, Pan, B, Mackay, JP, Mullen, GP and Rothfield, LI (1999) The dimerization and topological specificity functions of MinE reside in a structurally autonomous C-terminal domain. Mol. Microbiol. 31:1161-9 |
|---|---|
| Abstract |
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 alpha and beta 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 alpha-helical conformations. This suggests that the N-terminal region of MinE may be poised to adopt an alpha-helical conformation when it interacts with the target of its anti-MinCD activity, presumably MinD. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cell Cycle Proteins; Circular Dichroism; Dimerization; Escherichia coli/chemistry; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins; Magnetic Resonance Spectroscopy; Mass Spectrometry; Molecular Sequence Data; Protein Structure, Secondary; Structure-Activity Relationship; Substrate Specificity; Ultracentrifugation |
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