ABSTRACT: Bacterial cell division by binary fission is a tightly regulated process whereby the machinery responsible for physically dividing the cell is only allowed to form in the cell middle. In gram-negative strains of bacteria, there is a system comprised of three Min proteins that work together to allow the cell to ‘find the middle’ for this purpose. These proteins form dynamic long-range patterns on the cell membrane, creating waves that oscillate back and forth between the cell poles to sweep out an area that is permissive to division. Underlying these dynamics are protein-protein and protein-membrane interactions that we seek to understand at the molecular level. We have characterized dramatic conformational transformations in these proteins that are critical for this function. In this talk I will describe these structural transitions, and how they influence the Min protein function and the pattern formation that is critical for its function in the regulation of cell division.
Natalie obtained her PhD from the University of Toronto in 2001, followed by a postdoctoral fellowship at the Scripps Research Institute. She joined the Department of Chemistry at the University of Ottawa in 2003, using solution NMR to study structure/function relationships of proteins that work at the cell membrane. Targets include rhomboid intramembrane proteases, and the Min family of bacterial cell division proteins that self-organize to form dynamic patterns on membrane surfaces. She is a recipient of the John Charles Polanyi Prize in Chemistry, a Research Corporation Innovation Award, an Early Researcher Award and an NSERC Discovery Accelerator Supplement Award.