Recombinant Escherichia coli Cell division topological specificity factor (minE)

1. This review summarizes the cell-free data supporting a molecular mechanism that explains the variety of patterns supported by MinD and MinE both in and out of the cell; with an emphasis on the recent appreciation for how multiple conformational states of MinE can drive oscillation by spatiotemporally regulating MinD interaction with the membrane. PMID: 29188788
2. the dynamic association of the MTS with the beta-sheet is fine-tuned to balance MinE's need to sense MinD on the membrane with its need to diffuse in the cytoplasm, both of which are necessary for the oscillation PMID: 28652337
3. Non-linear Min protein interactions generate harmonics that signal mid-cell division in Escherichia coli. PMID: 29040283
4. membrane targeting sequence defines the lower limit of the concentration-dependent wavelength of Min protein patterns while restraining MinE's ability to stimulate MinD's ATPase activity. PMID: 28622374
5. Two MinD mutant proteins, MinD(K11A) and MinD(DeltaMTS15), are unable to form polymers with MinC PMID: 25497011
6. The MinCDE proteins prevent the formation of the Z-ring at poles by oscillating from pole to pole, thereby ensuring that the concentration of the Z-ring inhibitor, MinC, is lowest at the cell center. PMID: 24327341
7. MinD and MinE interact with anionic phospholipids and regulate division plane formation in Escherichia coli PMID: 23012351
8. The authors find that N45 in MinD is essential for MinE-stimulated ATPase activity and suggest that it is a key residue affected by MinE binding. PMID: 22651575
9. MinE shares common protein signatures with a group of membrane trafficking proteins in eukaryotic cells. These MinE signatures appear to affect membrane curvature. PMID: 21738659
10. These results identify the MinD-dependent conformational changes in MinE that convert it from a latent to an active form and lead to a model of how MinE persists at the MinD-membrane surface. PMID: 21816275
11. The binding sites for MinC and MinE overlap and reveals that they are at the MinD dimer interface. PMID: 21231967
12. polymerization of MinE over MinD oligomers triggers dynamic instability leading to detachment from the membrane. PMID: 20212106
13. report on stochastic switching of the MinD and MinE-protein distributions between the two cell halves in short Escherichia coli cells. PMID: 20308588
14. MinE and the invariant Lys11 residue in the ATPase P-loop of MinD compete for binding to a common site within the MinD structure, thereby providing a plausible structural basis for the ability of MinE to activate the ATPase activity of MinD. PMID: 15458408
15. Lysine 11 of MinD is required for interaction MinE; the three residues in helix 7 that interact with lysine 11 are not required for MinE binding but are required for MinE to stimulate the MinD ATPase PMID: 15629934
16. simple five-reaction model of the Min system can explain all documented Min phenotypes, if stochastic kinetics and three-dimensional diffusion are accounted for PMID: 16846247
17. In vivo measurements of the mobility of MinD and MinE using fluorescence correlation spectroscopy shows 2 distinct timescales; the diffusion constant of cytoplasmic MinE to be approximately 10 microm(2) s(-1) PMID: 17200601
18. Min proteins undergo a periodic pole-to-pole oscillation that involves polymerization and ATPase activity of MinD under the PMID: 17483175
19. MinCDE most often moved from one branch to another in an invariant order, following a nonreversing clockwise or counterclockwise direction over the time periods observed. PMID: 18178745

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KEGG: ecj:JW1163

STRING: 316385.ECDH10B_1227