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research article

A molecular device for the redox quality control of GroEL/ES substrates

Dupuy, Emile
•
Van der Verren, Sander Egbert
•
Lin, Jiusheng
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2023
Cell

Hsp60 chaperonins and their Hsp10 cofactors assist protein folding in all living cells, constituting the paradigmatic example of molecular chaperones. Despite extensive investigations of their structure and mechanism, crucial questions regarding how these chaperonins promote folding remain unsolved. Here, we report that the bacterial Hsp60 chaperonin GroEL forms a stable, functionally relevant complex with the chaperedoxin CnoX, a protein combining a chaperone and a redox function. Binding of GroES (Hsp10 cofactor) to GroEL induces CnoX release. Cryoelectron microscopy provided crucial structural information on the GroEL-CnoX complex, showing that CnoX binds GroEL outside the substrate-binding site via a highly conserved C-terminal α-helix. Furthermore, we identified complexes in which CnoX, bound to GroEL, forms mixed disulfides with GroEL substrates, indicating that CnoX likely functions as a redox quality-control plugin for GroEL. Proteins sharing structural features with CnoX exist in eukaryotes, suggesting that Hsp60 molecular plugins have been conserved through evolution.

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Type
research article
DOI
10.1016/j.cell.2023.01.013
Author(s)
Dupuy, Emile
•
Van der Verren, Sander Egbert
•
Lin, Jiusheng
•
Wilson, Mark Alan
•
Dachsbeck, Alix Vincent
•
Viela, Felipe
•
Latour, Emmanuelle
•
Gennaris, Alexandra
•
Vertommen, Didier
•
Dufrêne, Yves Frédéric
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Date Issued

2023

Published in
Cell
Volume

186

Issue

5

Start page

1039

End page

1049.e17

Subjects

protein folding

•

chaperones

•

redox

•

proteostasis

•

TPR

•

thioredoxin

•

chaperonin

Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
UPGOEMANS  
Available on Infoscience
September 19, 2023
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/200795
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