Abstract
FtsN is the last essential protein that is recruited to the septum before the onset of cell constriction. It is believed that FtsN triggers the septal peptidoglycan synthesis so as to initiate the cell constriction. However, the mechanisms behind it are unclear. Here we studied the dynamics of FtsN by using the combination of single molecule tracking (SMT), total internal reflection fluorescence structured illumination microscopy (TRIF-SIM), and fluorescence recovery after photobleaching (FRAP). Mutagenesis was also utilized to study the interaction partner which contributed to FtsN's dynamics.
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