Leigh G. Monahan,1,2
Peter L. Beech,3 and
Elizabeth J. Harry1,2*
School of Molecular and Microbial Biosciences, University of Sydney, Sydney, NSW, Australia,1 Institute for the Biology of Infectious Diseases, University of Technology, Sydney, NSW, Austrailia,2 School of Biological and Chemical Sciences, Deakin University, Burwood, VIC, Australia3
Received 30 August 2005/ Accepted 12 October 2005
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.
Supplemental material for this article may be found at http://jb.asm.org/.
Present address: MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
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