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Related Experiment Video

Updated: Jun 10, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

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Published on: January 11, 2017

DivIC stabilizes FtsL against RasP cleavage.

Inga Wadenpohl¹, Marc Bramkamp

¹Institute for Biochemistry, University of Cologne, Zülpicher Str. 47, Cologne D-50674, Germany.

Journal of Bacteriology

|July 21, 2010

Summary

The cell division protein FtsL is degraded by the protease RasP, but the protein DivIC protects FtsL from this cleavage. This stabilization prevents FtsL degradation, ensuring proper cell division.

Area of Science:

Molecular biology
Cell biology
Microbiology

Background:

FtsL is an essential protein for bacterial cell division.
RasP is an intramembrane protease that targets FtsL.
Regulation of FtsL levels is critical for cell division.

Purpose of the Study:

To investigate the interaction between FtsL and DivIC.
To determine how DivIC affects FtsL stability and degradation by RasP.
To elucidate the mechanism of FtsL regulation during cell division.

Main Methods:

Heterologous coexpression of FtsL and DivIC in a bacterial system.
Analysis of FtsL protein levels and degradation products.
Identification of substrate recognition motifs involved in RasP cleavage.

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Main Results:

DivIC significantly stabilizes FtsL against RasP-mediated cleavage.
Degradation of FtsL is initiated when a cytosolic recognition motif becomes accessible.
Coexpression of DivIC prevents FtsL degradation by RasP.

Conclusions:

DivIC plays a crucial role in protecting FtsL from degradation by RasP.
The accessibility of a cytosolic motif regulates FtsL degradation.
This interaction is essential for maintaining FtsL levels and ensuring proper cell division.