The FtsZ Protein of Bacillus Subtilis Is Localized at the Division Site and Has GTPase Activity That Is Dependent Upon FtsZ Concentration

Mol Microbiol. 1993 Aug;9(3):435-42. doi: 10.1111/j.1365-2958.1993.tb01705.x.

Abstract

The ftsZ gene is essential for cell division in both Escherichia coli and Bacillus subtilis. In E. coli FtsZ forms a cytokinetic ring at the division site whose formation is under cell-cycle control. In addition, the FtsZ from E. coli has a GTPase activity that shows an unusual lag in vitro. In this study we show that FtsZ in Bacillus subtilis forms a ring that is at the tip of the invaginating septum. The FtsZ ring is dynamic since it is formed as division is initiated, changes diameter during septation, and disperses upon completion of septation. In vitro the purified FtsZ from B. subtilis exhibits a GTPase activity without a demonstrable lag, but the GTPase activity is markedly dependent upon the FtsZ concentration, suggesting that the FtsZ protein must oligomerize to express the GTPase activity.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacillus subtilis / enzymology
  • Bacillus subtilis / growth & development*
  • Bacillus subtilis / ultrastructure
  • Bacterial Proteins / isolation & purification*
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / radiation effects
  • Cell Division
  • Cross-Linking Reagents
  • Cytoskeletal Proteins*
  • Escherichia coli / enzymology
  • Escherichia coli / growth & development
  • GTP Phosphohydrolases / isolation & purification*
  • GTP Phosphohydrolases / metabolism
  • GTP Phosphohydrolases / radiation effects
  • Guanosine Triphosphate / metabolism
  • Microscopy, Immunoelectron
  • Protein Conformation
  • Ultraviolet Rays

Substances

  • Bacterial Proteins
  • Cross-Linking Reagents
  • Cytoskeletal Proteins
  • FtsZ protein, Bacteria
  • Guanosine Triphosphate
  • GTP Phosphohydrolases