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Related Experiment Videos

An essential protease involved in bacterial cell-cycle control

U Jenal1, T Fuchs

  • 1Division of Molecular Microbiology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland. jenal@ubaclu.unibas.ch

The EMBO Journal
|October 2, 1998
PubMed
Summary

The bacterial protease ClpXP is vital for cell division and cell-cycle progression in Caulobacter crescentus. Its activity degrades the CtrA protein, enabling DNA replication and cell cycle transitions.

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Area of Science:

  • Microbiology
  • Cell Biology
  • Biochemistry

Background:

  • Proteolytic inactivation of regulatory proteins is crucial for eukaryotic cell-cycle control.
  • The role of proteolysis in bacterial cell-cycle regulation remains less understood.

Purpose of the Study:

  • To investigate the role of proteolysis in bacterial cell-cycle control.
  • To identify key proteases involved in Caulobacter crescentus cell-cycle progression.

Main Methods:

  • Identification and characterization of the ClpXP protease in Caulobacter crescentus.
  • Site-directed mutagenesis to assess the proteolytic activity of ClpP.
  • Analysis of ClpX and ClpP deletion mutants to study in vivo protein degradation and cell-cycle phenotypes.

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Main Results:

  • Mutants lacking the ATP-dependent serine protease ClpXP are arrested in the cell cycle before DNA replication and cell division.
  • ClpXP is essential for the cell-cycle-dependent degradation of the regulatory protein CtrA.
  • Proteolytic activity of ClpXP is required for CtrA degradation and cell-cycle progression.

Conclusions:

  • Proteolysis by ClpXP is indispensable for Caulobacter crescentus viability and cell-cycle progression.
  • Degradation of CtrA by ClpXP facilitates the G1-to-S transition by relieving its negative control on DNA replication.