My laboratory focuses on developing novel single-molecule imaging tools in live cells to probe various aspects of microbial cellular processes. We are broadly interested in understanding how the molecular constituents of bacterial cellular processes are spatially organized and what essential functions such an organization conveys. In this talk, I will discuss our recent work on the structure, function, and dynamics of the bacterial cell division machinery. Using single-molecule imaging in live E. coli cells, we first illustrated the structural organization of the bacterial cytokinesis ring formed by the tubulin homolog FtsZ protein. We next found that FtsZ uses its GTP hydrolysis to power treadmilling dynamics and function as a linear motor to transport sPG synthase enzymes evenly along the septum to ensure smooth, symmetric septum formation. We discovered that the activity of these enzymes is spatially regulated through their differential coupling to two distinct tracks along the septum. Through structural investigations, we provided molecular details of how the core division complex activates the essential sPG synthase complex. Our work point opens new directions to study the precise spatial coordination and regulation of the large ensemble of cell division proteins.

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