A new assembly pathway for the cytokinetic Z ring from a dynamic helical structure in vegetatively growing cells of Bacillus subtilis

Blackwell Publishing
Publication Type:
Journal Article
Molecular Microbiology, 2007, 64 (2), pp. 487 - 499
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The earliest event in bacterial cell division is the formation of a Z ring, composed of the tubulin-like FtsZ protein, at the division site at midcell. This ring then recruits several other division proteins and together they drive the formation of a division of septum between two replicated chromosomes. Here we show that, in addition to forming a cytokinetic ring, FtsZ localises in a helical-like pattern in vegetatively growing cells of Bacillus subtilis. FtsZ moves rapudly within this helix-like structure. Examination of FtsZ localisation in individual live cells undergoing a single cell cycle suggests a new assembly mechanism for Z ring formation tha involves a cell cycle-mediated multistep remodelling of FtsZ polymers. Our observations suggest that initially FtsZ localises in a helical pattern, with movement of FtsZ within this sturcture occurring along the entire length of the cell. Next, movement of FtsZ in a helical-like pattern is restricted to a central region of the cell. Finally the FtsZ ring forms precisely at midcell. We further show that another division protein, FtsA, shown to interact with FtsZ prior to Z ring formation in B. subtilis, also localises to similar helical patterns in vegetatively growing cells.
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