The dimerization and topological specificity functions of MinE reside in a structurally autonomous C-terminal domain. King, G., Rowland, S., Pan, B., Mackay, J., Mullen, G., & Rothfield, L. Molecular Microbiology, 31(4):1161-1169, 1999.
doi  abstract   bibtex   
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.
@article{
 title = {The dimerization and topological specificity functions of MinE reside in a structurally autonomous C-terminal domain},
 type = {article},
 year = {1999},
 pages = {1161-1169},
 volume = {31},
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 last_modified = {2023-01-10T01:46:43.487Z},
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 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 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.},
 bibtype = {article},
 author = {King, G.F. and Rowland, S.L. and Pan, B. and Mackay, J.P. and Mullen, G.P. and Rothfield, L.I.},
 doi = {10.1046/j.1365-2958.1999.01256.x},
 journal = {Molecular Microbiology},
 number = {4}
}

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