Journal
ANNUAL REVIEW OF MICROBIOLOGY
Volume 57, Issue -, Pages 125-154Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.micro.57.012903.074300
Keywords
cytokinesis; cytoskeleton; polymerization; cell cycle; tubulin
Categories
Funding
- NIGMS NIH HHS [R01 GM064671-02, R01 GM064671, R01 GM064671-03] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM064671] Funding Source: NIH RePORTER
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FtsZ is a prokaryotic tubulin homolog that assembles into a ring at the future site of cell division. The resulting Z ring forms the framework for the division apparatus, and its assembly is regulated throughout the bacterial cell cycle. A highly dynamic structure, the Z ring exhibits continual subunit turnover and the ability to rapidly assemble, disassemble, and, under certain circumstances, relocalize. These in vivo properties are ultimately due to FtsZ's capacity for guanosine triphosphate (GTP)-dependent, reversible polymerization. FtsZ polymer stability appears to be fine-tuned such that subtle changes in its assembly kinetics result in large changes in the Z ring structure. Thus, regulatory proteins that modulate FtsZ's assembly dynamics can cause the ring to rapidly remodel in response to developmental and environmental cues.
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