The polymerization mechanism of the bacterial cell division protein FtsZ

FEBS Lett. 2001 Sep 28;506(1):6-10. doi: 10.1016/s0014-5793(01)02855-1.

Abstract

Bacteria and archaea usually divide symmetrically by formation of a septum in the middle of the cell. A key event in cell division is the assembly of the FtsZ ring. FtsZ is the prokaryotic homolog of tubulin and forms polymers in the presence of guanine nucleotides. Here, we specifically address the polymerization of FtsZ and the role of nucleotide hydrolysis in polymer formation and stabilization. Recent structural and biochemical results are discussed and a model for FtsZ polymerization, similar to that for tubulin, is presented.

Publication types

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

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / physiology*
  • Biopolymers
  • Cytoskeletal Proteins*
  • Guanosine Triphosphate / metabolism
  • Hydrolysis
  • Models, Molecular
  • Protein Conformation
  • Tubulin / chemistry

Substances

  • Bacterial Proteins
  • Biopolymers
  • Cytoskeletal Proteins
  • FtsZ protein, Bacteria
  • Tubulin
  • Guanosine Triphosphate