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 Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Zhou, H. Articles by Lutkenhaus, J. Search for Related Content PubMed PubMed Citation Articles by Zhou, H. Articles by Lutkenhaus, J.

Analysis of MinD Mutations Reveals Residues Required for MinE Stimulation of the MinD ATPase and Residues Required for MinC Interaction

Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, Kansas

Received 25 June 2004/ Accepted 14 October 2004

The MinD ATPase is critical to the oscillation of the Min proteins, which limits formation of the Z ring to midcell. In the presence of ATP, MinD binds to the membrane and recruits MinC, forming a complex that can destabilize the cytokinetic Z ring. MinE, which is also recruited to the membrane by MinD, displaces MinC and stimulates the MinD ATPase, resulting in the oscillation of the Min proteins. In this study we have investigated the role of lysine 11, present in the deviant Walker A motif of MinD, and the three residues in helix 7 (E146, S148, and D152) that interact electrostatically with lysine 11. Lysine 11 is required for interaction of MinD with the membrane, MinC, MinE, and itself. In contrast, the three residues in helix 7 that interact with lysine 11 are not required for binding to the membrane or activation of MinC. They are also not required for MinE binding; however, they are required for MinE to stimulate the MinD ATPase. Interestingly, the D152A mutant self-interacts, binds to the membrane, and recruits MinC and MinE in the presence of ADP as well as ATP. This mutant provides evidence that dimerization of MinD is sufficient for MinD to bind the membrane and recruit its partners.

This article has been cited by other articles:

• Maple, J., Moller, S. G. (2007). Interdependency of formation and localisation of the Min complex controls symmetric plastid division. J. Cell Sci. 120: 3446-3456 [Abstract] [Full Text]  
• Cytrynbaum, E. N., Marshall, B. D. L. (2007). A Multistranded Polymer Model Explains MinDE Dynamics in E. coli Cell Division. Biophys. J 93: 1134-1150 [Abstract] [Full Text]  
• Soulat, D., Jault, J.-M., Duclos, B., Geourjon, C., Cozzone, A. J., Grangeasse, C. (2006). Staphylococcus aureus Operates Protein-tyrosine Phosphorylation through a Specific Mechanism. J. Biol. Chem. 281: 14048-14056 [Abstract] [Full Text]