NEW INFORMATION ABOUT THE STRUCTURES FORMED BY FtsZ PROTEIN
IN ESCHERICHIA COLI CELLS DURING DIVISION PROCESS OBTAINED
BY SINGLE-MOLECULE LOCALIZATION MICROSCOPY
A.D. Vedyaykin,1 I.E. Vishnyakov,1,2 V.S. Polinovskaya,1 T.O. Artamonova,1 M.A. Khodorkovskii,1 A.V. Sabantsev 1,*
1 Peter the Great St. Petersburg Polytechnic University, 195251,
and 2 Institute of Cytology RAS, St. Petersburg, 194064;
* e-mail: sabantsev.a.v.@gmail.com
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.
Key words:
single-molecule localization microscopy, sample position stabilization system, Escherichia coli, cytokinesis, FtsZ, contractile ring
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