1. Topological Regulation of Cell Division in E. coli
Zonglin Hu, Joe Lutkenhaus 
Molecular Cell 
Volume 7, Issue 6, Pages (June 2001)
DOI: /S (01)

2. Figure 1
MinE Stimulates MinD ATPase Activity in the Presence of Phospholipids
(A) MinD (16 μM) was incubated in buffer with 1 mM [32P]-γATP, and the amount of 32P released was determined. In some reactions, MinE (16 μM), MalE-MinC (16 μM), or phospholipid vesicles (480 μg/ml) were added. The following abbreviations are used: D, MinD; E, MinE, C, MinC; pl, phospholipid.
(B) The specific activity of the MinD ATPase was determined as a function of the MinD concentrations. All reactions were in the presence of MinE (16 μM) and phospholipid vesicles (480 μg/ml).
(C) Stimulation of the MinD ATPase depends on the MinE concentration. The effect of the concentration of MinE on the stimulation of the ATPase activity of MinD at 480 μg/ml (16 μM) was examined in the presence of phospholipid vesicles (480 μg/ml)
Molecular Cell 2001 7, DOI: ( /S (01) )

3. Figure 2 Phenotype of MinE Mutants Constructed in This Study
(A) Diagram indicating the amino acids substitutions in the various MinE mutants. Each mutant was tested for MinE function; the test involved prevention of MinCD induced filamentation: (+) indicates that MinE function was retained, and (−) indicates no MinE function. Each mutant was also tested for stability following overproduction: (+) indicates the mutant protein is stable, and (−) indicates that it is unstable.
(B) Effect of MinE mutants on MinD's ATPase activity. Each of the purified MinE mutant proteins was tested for its ability to stimulate MinD's ATPase activity. The concentration of the MinE mutant proteins was 2.4 μM. MinD was 16 μM, and phospholipids were 480 μg/ml
Molecular Cell 2001 7, DOI: ( /S (01) )

4. Figure 3 Behavior of GFP-MinD in the Presence of MinE Mutants
Each of the minE mutations was cloned downstream of gfp-minD under the control of the lac promoter. Each panel contains a phase contrast image followed by one or more fluorescent images. In cases in which there is more than one image, they were photographed 25 s apart.
(A) Wild-type MinE.
(B) MinE6.
(C) MinE7.
(D) MinE2.
(E) MinE4.
(F) MinE3.
(G) MinE8
Molecular Cell 2001 7, DOI: ( /S (01) )

5. Figure 4 Model for MinE Stimulation of MinD Oscillation
(A) MinD oligomerizes in response to ATP. Membrane-bound MinD hydrolyzes ATP in response to MinE; it then dissociates from the membrane.
(B) Model for oscillation. The MinE ring is indicated at the end of the MinD, where it stimulates MinD ATPase activity causing release of MinD from the membrane. MinC is not shown but is assumed to be associated with MinD at the membrane. As MinD is released, it diffuses in the cytoplasm and initiates assembly at the opposite cell pole. As the MinE ring reaches the pole, it is released and reforms at the growing end of the MinD horseshoe emanating from the other pole, repeating the cycle
Molecular Cell 2001 7, DOI: ( /S (01) )