Format

Send to

Choose Destination
Biophys J. 2014 Oct 21;107(8):L17-L20. doi: 10.1016/j.bpj.2014.08.024.

3D-SIM super-resolution of FtsZ and its membrane tethers in Escherichia coli cells.

Author information

1
Department of Microbiology and Molecular Genetics, University of Texas Medical School at Houston, Houston, Texas.
2
Department of Microbiology and Molecular Genetics, University of Texas Medical School at Houston, Houston, Texas. Electronic address: william.margolin@uth.tmc.edu.

Abstract

FtsZ, a bacterial homolog of eukaryotic tubulin, assembles into the Z ring required for cytokinesis. In Escherichia coli, FtsZ interacts directly with FtsA and ZipA, which tether the Z ring to the membrane. We used three-dimensional structured illumination microscopy to compare the localization patterns of FtsZ, FtsA, and ZipA at high resolution in Escherichia coli cells. We found that FtsZ localizes in patches within a ring structure, similar to the pattern observed in other species, and discovered that FtsA and ZipA mostly colocalize in similar patches. Finally, we observed similar punctate and short polymeric structures of FtsZ distributed throughout the cell after Z rings were disassembled, either as a consequence of normal cytokinesis or upon induction of an endogenous cell division inhibitor.

PMID:
25418183
PMCID:
PMC4213660
DOI:
10.1016/j.bpj.2014.08.024
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center