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Updated: Jul 5, 2026

Measuring the Bending Stiffness of Bacterial Cells Using an Optical Trap

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Published on: April 26, 2010

A stress sensor for the bacterial periplasm.

Jason C Young¹, F Ulrich Hartl

¹Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany.

|April 8, 2003

Summary

DegS, a periplasmic stress sensor, activates upon recognizing misfolded outer membrane porins. This triggers a cascade, enhancing cellular protection through chaperone production.

Area of Science:

Microbiology
Cellular Biology
Protein Degradation

Background:

The periplasm is a critical cellular compartment housing essential proteins.
Outer membrane porins are vital for nutrient transport but can misfold.
Periplasmic stress responses are crucial for maintaining cellular homeostasis.

Purpose of the Study:

To elucidate the activation mechanism of the DegS protease.
To understand the role of DegS in the sigma(E) stress response pathway.
To investigate the interaction between DegS and outer membrane porins.

Main Methods:

Biochemical assays to study protein-protein interactions.
Proteolysis assays to measure DegS protease activity.
Genetic analysis of the sigma(E) pathway.

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Last Updated: Jul 5, 2026

Measuring the Bending Stiffness of Bacterial Cells Using an Optical Trap

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Published on: April 26, 2010

Stress-induced Antibiotic Susceptibility Testing on a Chip

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Published on: January 8, 2014

Measurements of Physiological Stress Responses in C. Elegans

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Published on: May 21, 2020

Main Results:

DegS activation is mediated by the recognition of misfolded outer membrane porins via its PDZ domain.
This recognition event allosterically activates the DegS protease domain.
Activated DegS initiates a proteolytic cascade leading to sigma(E) activation.

Conclusions:

DegS acts as a key sensor of outer membrane protein stress.
The DegS-mediated cascade is essential for inducing the sigma(E) regulon.
This pathway ensures the production of periplasmic chaperones to resolve stress.