[NEW INFORMATION ABOUT THE STRUCTURES FORMED BY FtsZ PROTEIN IN ESCHERICHIA COLI CELLS DURING DIVISION PROCESS OBTAINED BY SINGLE-MOLECULE LOCALIZATION MICROSCOPY].

FtsZ--a bacterial tubulin homolog--is one of the key bacterial division proteins, forming a contractile Z-ring at the midcell of dividing bacteria. In this work immunofluorescent labeling was used in conjunction with single-molecule localization microscopy (SMLM) to visualize native structures formed by FtsZ protein in Escherichia coli cells. This approach allowed the reorganization of FtsZ structures during cytokinesis to be visualized step-by-step. New data was obtained that support the hypothesis that the Z-ring is a spiral structure that constricts during division, assisting the formation of the septum between daughter cells.