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Related Experiment Videos

Immediate GTP hydrolysis upon FtsZ polymerization.

Dirk-Jan Scheffers1, Arnold J M Driessen

  • 1Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9750 NN Haren, The Netherlands. dirk-jan.scheffers@pathology.ox.ac.uk

Molecular Microbiology
|April 16, 2002
PubMed
Summary

FtsZ polymerization dynamics were studied. Radiolabeled GTP instantly hydrolyzes upon FtsZ polymerization, indicating polymers contain GDP and inorganic phosphate, not GTP.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • FtsZ is a bacterial cell division protein analogous to tubulin.
  • Understanding FtsZ polymerization requires knowing the bound nucleotide state.
  • Previous studies conflict on whether polymerized FtsZ binds GDP or GTP.

Purpose of the Study:

  • To resolve the nucleotide-bound state of FtsZ polymers.
  • To investigate the immediate consequences of GTP binding during FtsZ polymerization.

Main Methods:

  • Polymerization of FtsZ using radiolabeled [gamma-32P]-GTP.
  • Analysis of nucleotide and phosphate content within FtsZ polymers.

Main Results:

  • Guanosine triphosphate (GTP) is instantaneously hydrolyzed during FtsZ polymerization.

Related Experiment Videos

  • FtsZ polymers were found to contain guanosine diphosphate (GDP).
  • The radiolabeled inorganic phosphate (32P) was detected within the FtsZ polymer.

    • Conclusions:

    • The FtsZ polymer primarily contains GDP, not GTP.
    • Instantaneous GTP hydrolysis is a key feature of FtsZ polymerization dynamics.
    • This finding clarifies the nucleotide state crucial for bacterial cell division.