Friday, April 13, 2018 - 12:00pm - 1:00pm
Hugel 100
Ryan McQuillen
Bacterial cell division is an essential process mediated by the highly-conserved prokaryotic tubulin homolog GTPase FtsZ. Early in division, FtsZ forms a cytokinetic ring (the Z-ring) at midcell and recruits all other downstream factors which coordinate constriction and nucleoid segregation.  While it is clear that FtsZ is required for successful cell division, its mechanistic role(s) represent an active area of investigation. Recent work in our lab shows that, FtsZ polymers treadmill about the midcell region in a manner correlated with FtsZ’s intrinsic GTPase activity. We also observed that FtsI (PBP3) undergoes directional movement and that its speed is correlated with that of FtsZ. We therefore hypothesize that the dynamic motion of FtsZ is required to regulate the spatiotemporal distributions of cell wall remodeling enzymes during constriction. However, how imperative the requirement for FtsZ is during constriction is still not well understood.
In an attempt to better understand FtsZ’s role during constriction, we are currently developing a method to rapidly disassemble the Z-ring at different time points over the course of the cell cycle and examine the consequences in the localization, function and dynamics of other divisome components. Our method uses variants of a pair of proteins, CRY2 and CIB1, isolated from Arabidopsis thaliana. Fusions of these proteins have been shown to rapidly dimerize upon irradiation with 488nm light in mammalian cells. To our knowledge, this system has yet to be applied in bacteria and may represent an effective method to shed light on a number of questions.
Sponsored by: 
Physics Department

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Scott Shelley