The tubulin ancestor, FtsZ, draughtsman, designer and driving force for bacterial cytokinesis

J Mol Biol. 2002 Apr 26;318(2):219-36. doi: 10.1016/S0022-2836(02)00024-4.

Abstract

We discuss in this review the regulation of synthesis and action of FtsZ, its structure in relation to tubulin and microtubules, and the mechanism of polymerization and disassembly (contraction) of FtsZ rings from a specific nucleation site (NS) at mid cell. These topics are considered in the light of recent immunocytological studies, high resolution structures of some division proteins and results indicating how bacteria may measure their mid cell point.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacteria / genetics*
  • Bacteria / growth & development*
  • Bacterial Physiological Phenomena
  • Bacterial Proteins / antagonists & inhibitors
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / physiology*
  • Caulobacter crescentus / genetics
  • Caulobacter crescentus / growth & development
  • Caulobacter crescentus / physiology
  • Cell Cycle
  • Cell Division
  • Cytoskeletal Proteins*
  • Escherichia coli / genetics
  • Escherichia coli / growth & development
  • Escherichia coli / physiology
  • GTP Phosphohydrolases / metabolism
  • Genes, Bacterial
  • Methanococcus / chemistry
  • Microtubules / physiology
  • Models, Molecular
  • Tubulin / genetics*
  • Tubulin / physiology*

Substances

  • Bacterial Proteins
  • Cytoskeletal Proteins
  • FtsZ protein, Bacteria
  • MinC protein, Bacteria
  • Tubulin
  • GTP Phosphohydrolases