Trapping of a spiral-like intermediate of the bacterial cytokinetic protein FtsZ

Publication Type:
Journal Article
Journal of Bacteriology, 2006, 188 (5), pp. 1680 - 1690
Issue Date:
Filename Description Size
Thumbnail2006003930.pdf1.47 MB
Adobe PDF
Full metadata record
The earliest stage in bacterial cell division is the formation of a ring, composed of the tubulin-like protein FtsZ, at the division site. Tight spatial and temporal regulation of Z-ring formation is required to ensure that division occurs precisely at midcell between two replicated chromosomes. However, the mechanism of Z-ring formation and its regulation in vivo remain unresolved. Here we identify the defect of an interesting temperature-sensitive ftsZ mutant (ts1) of Bacillus subtilis. At the nonpermissive temperature, the mutant protein, FtsZ(Ts1), assembles into spiral-like structures between chromosomes. When shifted back down to the permissive temperature, functional Z rings form and division resumes. Our observations support a model in which Z-ring formation at the division site arises from reorganization of a long cytoskeletal spiral form of FtsZ and suggest that the FtsZ(Ts1) protein is captured as a shorter spiral-forming intermediate that is unable to complete this reorganization step. The ts1 mutant is likely to be very valuable in revealing how FtsZ assembles into a ring and how this occurs precisely at the division site. Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Please use this identifier to cite or link to this item: