title: 3D-SIM super-resolution of FtsZ and its membrane tethers in Escherichia coli cells.
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.
authors.affiliation: Department of Microbiology and Molecular Genetics, University of Texas Medical School at Houston, Houston, Texas.
authors.forename: Veronica Wells
authors.initials: VW
authors.lastname: Rowlett
authors.affiliation: Department of Microbiology and Molecular Genetics, University of Texas Medical School at Houston, Houston, Texas. Electronic address: william.margolin@uth.tmc.edu.
authors.forename: William
authors.initials: W
authors.lastname: Margolin
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism* / Q000648:ultrastructure; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism* / Q000648:ultrastructure; D021621:Imaging, Three-Dimensional; D011485:Protein Binding
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria