The assembly of the divisome in E. coli occurs in two temporally distinct steps. In the first step, which is under spatial regulation, polymers of FtsZ ae attached to the membrane with the aid of FtsA and ZipA to form the Z ring. Additional nonessential FtsZ interacting proteins also join the Z ring at this time and contribute to the integrity of the Z ring. In a second step, seven additional essential proteins are added nearly simultaneously to form the divisome that divides the cell. In this grant we will focus on three aspects of the regulation of bacterial cell division. In the first aim we will test our Tarzan of te Jungle model for Min oscillation that contributes to the spatial regulation of the Z ring. In the second aim we will test our model for how FtsA is regulated to recruit late division proteins to the Z ring. This model proposes that FtsA's ability to recruit downstream division proteins to the Z ring is determined by its oligomeric state, which is regulated by the dynamics of proteins that interact with the conserved carboxy tail of FtsZ. Lastly, we will examine how a novel regulator, which we think represents a new regulatory aspect of FtsZ, affects FtsZ activity.

Public Health Relevance

The process of cytokinesis is essential to cellular life, and as such merits study. By continuing to unravel the mechanism of cytokinesis and the regulatory features used by the cell to control this process, it is anticipated that novel targets for the antibiotics will continue to emerge.

National Institute of Health (NIH)
National Institute of General Medical Sciences (NIGMS)
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Prokaryotic Cell and Molecular Biology Study Section (PCMB)
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Gindhart, Joseph G
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University of Kansas
Schools of Medicine
Kansas City
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Du, Shishen; Lutkenhaus, Joe (2014) SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD. PLoS Genet 10:e1004460
Pichoff, Sebastien; Shen, Bang; Sullivan, Bradley et al. (2012) FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins. Mol Microbiol 83:151-67
Shen, Bang; Lutkenhaus, Joe (2011) Differences in MinC/MinD sensitivity between polar and internal Z rings in Escherichia coli. J Bacteriol 193:367-76
Dajkovic, Alex; Pichoff, Sebastien; Lutkenhaus, Joe et al. (2010) Cross-linking FtsZ polymers into coherent Z rings. Mol Microbiol 78:651-68
Shen, Bang; Lutkenhaus, Joe (2010) Examination of the interaction between FtsZ and MinCN in E. coli suggests how MinC disrupts Z rings. Mol Microbiol 75:1285-98
Dajkovic, Alex; Lan, Ganhui; Sun, Sean X et al. (2008) MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ. Curr Biol 18:235-44
Pichoff, Sebastien; Lutkenhaus, Joe (2007) Identification of a region of FtsA required for interaction with FtsZ. Mol Microbiol 64:1129-38
Dajkovic, Alex; Lutkenhaus, Joe (2006) Z ring as executor of bacterial cell division. J Mol Microbiol Biotechnol 11:140-51
Zhou, Huaijin; Lutkenhaus, Joe (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 187:2846-57
Pichoff, Sebastien; Lutkenhaus, Joe (2005) Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Mol Microbiol 55:1722-34

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