Super-resolution imaging of the bacterial cytokinetic protein FtsZ

Elsevier B.V.
Publication Type:
Journal Article
Micron, 2011, 42 (4 Special Issue), pp. 336 - 341
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The idea of a bacterial cytoskeleton arose just 10 years ago with the identification of the cell division protein, FtsZ, as a tubulin homolog. Fts,Z plays a pivotal role in bacterial division, and is present in virtually all prokaryotes and in some eukaryotic organelles. The earliest stage of bacterial cell division is the assembly of FtsZ into a Z ring at the -division site, which subsequently constricts during cytokinesis. FtsZ also assembles into dynamic helical structures along the bacterial ceil, which are thought to act as precursors to the Z fing via a cell-cycle-mediated FtsZ polymer remodelling. The fine structures of the FtsZ helix and ring are unknown but crucial for identifying the molecular details of Z ring assembly and its regulation. We now reveal, using STED microscopy that the FtsZ helical structure in cells of the gram positive bacterium, Bacillus subtilis, is a highly irregular and discontinuous helix of FtsZ; very different to the smooth cable-like appearance observed by conventional fluorescence optics. STED also identifies a novel FtsZ helical structure of smaJ!er pitch that is invisible to standard optical methods, identifying a possible third intermediate in the pathway to Z ring assembly, which commits bacterial cells to divide.
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