This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Johnson, J. E. Articles by de Boer, P. A. J. Search for Related Content PubMed PubMed Citation Articles by Johnson, J. E. Articles by de Boer, P. A. J.

Targeting of ^DMinC/MinD and ^DMinC/DicB Complexes to Septal Rings in Escherichia coli Suggests a Multistep Mechanism for MinC-Mediated Destruction of Nascent FtsZ Rings

Department of Molecular Biology and Microbiology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4960

Received 16 January 2002/ Accepted 11 March 2002

The MinC protein is an important determinant of septal ring positioning in Escherichia coli. The N-terminal domain (^ZMinC) suppresses septal ring formation by interfering with FtsZ polymerization, whereas the C-terminal domain (^DMinC) is required for dimerization as well as for interaction with the MinD protein. MinD oscillates between the membrane of both cell halves in a MinE-dependent fashion. MinC oscillates along with MinD such that the time-integrated concentration of ^ZMinC at the membrane is minimal, and hence the stability of FtsZ polymers is maximal, at the cell center. MinC is cytoplasmic and fails to block FtsZ assembly in the absence of MinD, indicating that recruitment of MinC by MinD to the membrane enhances ^ZMinC function. Here, we present evidence that the binding of ^DMinC to MinD endows the MinC/MinD complex with a more specific affinity for a septal ring-associated target in vivo. Thus, MinD does not merely attract MinC to the membrane but also aids MinC in specifically binding to, or in close proximity to, the substrate of its ^ZMinC domain. MinC-mediated division inhibition can also be activated in a MinD-independent fashion by the DicB protein of cryptic prophage Kim. DicB shows little homology to MinD, and how it stimulates MinC function has been unclear. Similar to the results obtained with MinD, we find that DicB interacts directly with ^DMinC, that the ^DMinC/DicB complex has a high affinity for some septal ring target(s), and that MinC/DicB interferes with the assembly and/or integrity of FtsZ rings in vivo. The results suggest a multistep mechanism for the activation of MinC-mediated division inhibition by either MinD or DicB and further expand the number of properties that can be ascribed to the Min proteins.

This article has been cited by other articles:

• Bendezu, F. O., de Boer, P. A. J. (2008). Conditional Lethality, Division Defects, Membrane Involution, and Endocytosis in mre and mrd Shape Mutants of Escherichia coli. J. Bacteriol. 190: 1792-1811 [Abstract] [Full Text]  
• DeVito, J. A. (2008). Recombineering with tolC as a Selectable/Counter-selectable Marker: remodeling the rRNA Operons of Escherichia coli. Nucleic Acids Res 36: e4-e4 [Abstract] [Full Text]  
• Corbin, B. D., Wang, Y., Beuria, T. K., Margolin, W. (2007). Interaction between Cell Division Proteins FtsE and FtsZ. J. Bacteriol. 189: 3026-3035 [Abstract] [Full Text]  
• Shiomi, D., Margolin, W. (2007). The C-Terminal Domain of MinC Inhibits Assembly of the Z Ring in Escherichia coli. J. Bacteriol. 189: 236-243 [Abstract] [Full Text]  
• Zhou, H., Lutkenhaus, J. (2005). MinC Mutants Deficient in MinD- and DicB-Mediated Cell Division Inhibition Due to Loss of Interaction with MinD, DicB, or a Septal Component. J. Bacteriol. 187: 2846-2857 [Abstract] [Full Text]  
• Zhou, H., Schulze, R., Cox, S., Saez, C., Hu, Z., Lutkenhaus, J. (2005). Analysis of MinD Mutations Reveals Residues Required for MinE Stimulation of the MinD ATPase and Residues Required for MinC Interaction. J. Bacteriol. 187: 629-638 [Abstract] [Full Text]  
• Varma, A., Young, K. D. (2004). FtsZ Collaborates with Penicillin Binding Proteins To Generate Bacterial Cell Shape in Escherichia coli. J. Bacteriol. 186: 6768-6774 [Abstract] [Full Text]  
• Ramirez-Arcos, S., Greco, V., Douglas, H., Tessier, D., Fan, D., Szeto, J., Wang, J., Dillon, J. R. (2004). Conserved Glycines in the C Terminus of MinC Proteins Are Implicated in Their Functionality as Cell Division Inhibitors. J. Bacteriol. 186: 2841-2855 [Abstract] [Full Text]  
• Johnson, J. E., Lackner, L. L., Hale, C. A., de Boer, P. A. J. (2004). ZipA Is Required for Targeting of DMinC/DicB, but Not DMinC/MinD, Complexes to Septal Ring Assemblies in Escherichia coli. J. Bacteriol. 186: 2418-2429 [Abstract] [Full Text]  
• Zhou, H., Lutkenhaus, J. (2004). The Switch I and II Regions of MinD Are Required for Binding and Activating MinC. J. Bacteriol. 186: 1546-1555 [Abstract] [Full Text]  
• Szeto, T. H., Rowland, S. L., Habrukowich, C. L., King, G. F. (2003). The MinD Membrane Targeting Sequence Is a Transplantable Lipid-binding Helix. J. Biol. Chem. 278: 40050-40056 [Abstract] [Full Text]  
• Zhou, H., Lutkenhaus, J. (2003). Membrane Binding by MinD Involves Insertion of Hydrophobic Residues within the C-Terminal Amphipathic Helix into the Bilayer. J. Bacteriol. 185: 4326-4335 [Abstract] [Full Text]  
• Errington, J., Daniel, R. A., Scheffers, D.-J. (2003). Cytokinesis in Bacteria. Microbiol. Mol. Biol. Rev. 67: 52-65 [Abstract] [Full Text]  
• Lackner, L. L., Raskin, D. M., de Boer, P. A. J. (2003). ATP-Dependent Interactions between Escherichia coli Min Proteins and the Phospholipid Membrane In Vitro. J. Bacteriol. 185: 735-749 [Abstract] [Full Text]