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Molecular transformers in the cell: lessons learned from the DegP protease-chaperone
Justyna Sawa1, Alexander Heuck, Michael Ehrmann
1Research Institute of Molecular Pathology, Vienna, Austria.
Current Opinion in Structural Biology
|March 2, 2010
Summary
DegP protease undergoes oligomer reassembly upon binding unfolded proteins, forming a cage that degrades misfolded proteins and stabilizes native ones. This highlights DegP
Area of Science:
- Molecular Biology
- Protein Biochemistry
- Cellular Biology
Background:
- DegP is a crucial protease and chaperone involved in protein quality control.
- Understanding DegP's regulatory mechanism is key to comprehending cellular proteostasis.
Purpose of the Study:
- To elucidate the structure-function relationship and regulatory mechanism of DegP.
- To investigate DegP's role in the biogenesis of outer membrane proteins (OMPs).
Main Methods:
- Structure-function analysis of DegP.
- Oligomerization state studies under different protein binding conditions.
- Isolation and characterization of DegP-OMP complexes.
Main Results:
- Unfolded protein binding induces DegP hexamer (DegP6) to reassemble into a functional protease-chaperone dodecamer (DegP12/24).
- The DegP12/24 cage acts as a proteolytic folding chamber, degrading misfolded proteins and stabilizing native proteins.
- DegP plays a vital role in outer membrane protein biogenesis by stabilizing encapsulated OMP beta-barrels within its hydrophobic chamber.
Conclusions:
- DegP exhibits a novel substrate-induced oligomer conversion mechanism for protease and chaperone regulation.
- DegP's function in OMP biogenesis is analogous to chaperones assisting soluble protein folding.
- DegP represents a complex proteolytic machine regulated by stress-induced oligomer conversion.
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