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The Chaperonin TRiC/CCT Associates with Prefoldin through a Conserved Electrostatic Interface Essential for Cellular
Daniel Gestaut1, Soung Hun Roh2, Boxue Ma3
1Department of Biology and Genetics, Stanford University, Stanford, CA 94305, USA.
Cell
|April 9, 2019
Summary
The essential chaperones TRiC/CCT and prefoldin/GIMc (PFD) form a supra-chaperone assembly crucial for protein folding. This complex prevents toxic protein aggregation and maintains cellular proteostasis.
Area of Science:
- Molecular Biology
- Structural Biology
- Cell Biology
Background:
- Eukaryotic protein folding relies on chaperone systems like TRiC/CCT and prefoldin/GIMc (PFD).
- Understanding the cooperation between these chaperones is vital for maintaining proteostasis.
Purpose of the Study:
- To elucidate the structural and functional interplay between TRiC/CCT and PFD.
- To investigate the mechanism by which PFD enhances TRiC/CCT's protein folding activity.
Main Methods:
- Cryoelectron microscopy (cryo-EM) to determine the structure of the TRiC-PFD complex.
- Crosslinking-mass-spectrometry to map protein-protein interactions.
- Biochemical and cellular assays to assess functional consequences.
Main Results:
- TRiC/CCT and PFD associate via a conserved electrostatic interface, forming a defined architecture.
- PFD exhibits a conformational cycle between open and closed states, aligning substrate-binding chambers.
- PFD enhances TRiC/CCT folding rates and yields, suppressing non-productive cycles.
- Disruption of the TRiC-PFD interaction leads to amyloid aggregate accumulation in vivo.
Conclusions:
- The TRiC-PFD supra-chaperone assembly is essential for effective cellular proteostasis.
- This complex prevents toxic protein conformations and maintains protein folding fidelity.
- The interaction is critical for cellular health, with disruption causing deleterious effects.
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