Journal
MICRON
Volume 42, Issue 4, Pages 336-341Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.micron.2010.09.003
Keywords
STED; Super-resolution microscopy; FtsZ; Cell division; Bacillus subtilis
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Funding
- Australian Research Council
- National Health and Medical Research Council, Australia
- ARC FABLS network
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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. FtsZ 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 cell, which are thought to act as precursors to the Z ring 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 smaller 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. Crown Copyright (C) 2010 Published by Elsevier Ltd. All rights reserved.
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