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GENES & DEVELOPMENT 22:1741-1746, 2008
©2008 by Cold Spring Harbor Laboratory Press; ISSN 0890-9369/ $5.00
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RESEARCH COMMUNICATION

The bacterial cell division protein FtsZ assembles into cytoplasmic rings in fission yeast

Ramanujam Srinivasan1,4, Mithilesh Mishra1,4, Lifang Wu2, Zhongchao Yin2, and Mohan K. Balasubramanian1,3,5

1 Cell Division Laboratory, Temasek Life Sciences Laboratory, The National University of Singapore, Singapore 117604; 2 Molecular Plant Pathology, Temasek Life Sciences Laboratory, The National University of Singapore, Singapore 117604; 3 Department of Biological Sciences, The National University of Singapore, Singapore 117604

During cytokinesis, most bacteria assemble a ring-like structure that is composed of the tubulin homolog FtsZ. The mechanisms regulating assembly and organization of FtsZ molecules into rings are not fully understood. Here, we express bacterial FtsZ in the fission yeast Schizosaccharomyces pombe and find that FtsZ filaments assemble into cytoplasmic rings. Investigation of the Escherichia coli FtsZ revealed that ring assembly occurred by a process of closure and/or spooling of linear bundles. We conclude that FtsZ rings can assemble in the absence of all other bacterial cytokinetic proteins and that the process might involve hydrolysis of FtsZ-bound GTP and lateral associations between FtsZ filaments.

[Keywords: FtsZ; cytokinesis; tubulin; yeast]

Received February 7, 2008; revised version accepted May 5, 2008.

4 These authors contributed equally to this work.

5 Corresponding author.

E-MAIL mohan{at}tll.org.sg; FAX 65-6872-7012.

Supplemental material is available at http://www.genesdev.org.

Article is online at http://www.genesdev.org/cgi/doi/10.1101/gad.1660908.


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