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PMID:21097625
| Citation |
Shen, B and Lutkenhaus, J (2011) Differences in MinC/MinD sensitivity between polar and internal Z rings in Escherichia coli. J. Bacteriol. 193:367-76 |
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| Abstract |
In Escherichia coli the Z ring has the potential to assemble anywhere along the cell length but is restricted to midcell by the action of negative regulatory systems, including Min. In the current model for the Min system, the MinC/MinD division inhibitory complex is evenly distributed on the membrane and can disrupt Z rings anywhere in the cell; however, MinE spatially regulates MinC/MinD by restricting it to the cell poles, thus allowing Z ring formation at midcell. This model assumes that Z rings formed at different cellular locations have equal sensitivity to MinC/MinD in the absence of MinE. However, here we report evidence that differences in MinC/MinD sensitivity between polar and nonpolar Z rings exists even when there is no MinE. MinC/MinD at proper levels is able to block minicell production in Δmin strains without increasing the cell length, indicating that polar Z rings are preferentially blocked. In the FtsZ-I374V strain (which is resistant to MinC(C)/MinD), wild-type morphology can be easily achieved with MinC/MinD in the absence of MinE. We also show that MinC/MinD at proper levels can rescue the lethal phenotype of a min slmA double deletion mutant, which we think is due to the elimination of polar Z rings (or FtsZ structures), which frees up FtsZ molecules for assembly of Z rings at internal sites to rescue division and growth. Taken together, these data indicate that polar Z rings are more susceptible to MinC/MinD than internal Z rings, even when MinE is absent. |
| Links |
PubMed PMC3019829 Online version:10.1128/JB.01095-10 |
| Keywords |
Adenosine Triphosphatases/metabolism; Bacterial Proteins/antagonists & inhibitors; Bacterial Proteins/metabolism; Cell Cycle Proteins/metabolism; Cell Division; Cytoskeletal Proteins/antagonists & inhibitors; Cytoskeletal Proteins/metabolism; Escherichia coli/cytology; Escherichia coli/growth & development; Escherichia coli/physiology; Escherichia coli Proteins/metabolism; Membrane Proteins/metabolism; Microscopy; Protein Multimerization |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0005886: plasma membrane |
ECO:0000315: |
C |
The effect is very similar to SulA in that minicells are still produced at the level that causes mild filamentation (Fig. (Fig.2).2). These results indicate that MinD is not absolutely required for MinC to distinguish internal Z rings from polar Z rings but that MinC has to be on the membrane to achieve this effect. On the other hand, a wild-type morphology can be readily achieved with MinC/MinD but not with MinC-MTS, suggesting that MinD plays other roles in addition to recruiting MinC to the membrane. |
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See also
References
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