New insights into FtsZ rearrangements during the cell division of Escherichia coli from single-molecule localization microscopy of fixed cells

Microbiologyopen. 2016 Jun;5(3):378-86. doi: 10.1002/mbo3.336. Epub 2016 Feb 3.

Abstract

FtsZ - a prokaryotic tubulin homolog - is one of the central components of bacterial division machinery. At the early stage of cytokinesis FtsZ forms the so-called Z-ring at mid-cell that guides septum formation. Many approaches were used to resolve the structure of the Z-ring, however, researchers are still far from consensus on this question. We utilized single-molecule localization microscopy (SMLM) in combination with immunofluorescence staining to visualize FtsZ in Esherichia coli fixed cells that were grown under slow and fast growth conditions. This approach allowed us to obtain images of FtsZ structures at different stages of cell division and accurately measure Z-ring dimensions. Analysis of these images demonstrated that Z-ring thickness increases during constriction, starting at about 70 nm at the beginning of division and increasing by approximately 25% half-way through constriction.

Keywords: Divisome; FtsZ; Z-ring; single-molecule localization microscopy.

MeSH terms

  • Bacterial Proteins / genetics*
  • Cell Division / genetics*
  • Cell Division / physiology
  • Cytoskeletal Proteins / genetics*
  • Escherichia coli / genetics*
  • Escherichia coli / growth & development*
  • Fluorescent Antibody Technique, Indirect
  • Microscopy, Fluorescence
  • Tubulin / genetics

Substances

  • Bacterial Proteins
  • Cytoskeletal Proteins
  • FtsZ protein, Bacteria
  • Tubulin