Assembly dynamics of the bacterial cell division protein FTSZ: poised at the edge of stability

Annu Rev Microbiol. 2003;57:125-54. doi: 10.1146/annurev.micro.57.012903.074300.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Bacillus subtilis / metabolism
  • Bacillus subtilis / physiology
  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / metabolism*
  • Cell Division / physiology
  • Escherichia coli / metabolism
  • Escherichia coli / physiology
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / metabolism*
  • GTP-Binding Proteins / chemistry
  • GTP-Binding Proteins / metabolism
  • Guanosine Triphosphate / metabolism
  • Protein Conformation

Substances

  • Cell Cycle Proteins
  • Escherichia coli Proteins
  • FtsZ84 protein, E coli
  • Guanosine Triphosphate
  • GTP-Binding Proteins