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.
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.
|Pichoff, Sebastien; Du, Shishen; Lutkenhaus, Joe (2015) The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring. Mol Microbiol 95:971-87|
|Du, Shishen; Park, Kyung-Tae; Lutkenhaus, Joe (2015) Oligomerization of FtsZ converts the FtsZ tail motif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA. Mol Microbiol 95:173-88|
|Park, Kyung-Tae; Du, Shishen; Lutkenhaus, Joe (2015) MinC/MinD copolymers are not required for Min function. Mol Microbiol 98:895-909|
|Du, Shishen; Lutkenhaus, Joe (2014) SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD. PLoS Genet 10:e1004460|
|Du, Shishen; Lutkenhaus, Joe (2012) MipZ: one for the pole, two for the DNA. Mol Cell 46:239-40|
|Park, Kyung-Tae; Wu, Wei; Lovell, Scott et al. (2012) Mechanism of the asymmetric activation of the MinD ATPase by MinE. Mol Microbiol 85:271-81|
|Lutkenhaus, Joe (2012) The ParA/MinD family puts things in their place. Trends Microbiol 20:411-8|
|Lutkenhaus, Joe; Pichoff, Sebastien; Du, Shishen (2012) Bacterial cytokinesis: From Z ring to divisome. Cytoskeleton (Hoboken) 69:778-90|
|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|
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