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TitleA molecular device for the redox quality control of GroEL/ES substrates.
Journal, issue, pagesCell, Vol. 186, Issue 5, Page 1039-1049.e17, Year 2023
Publish dateMar 2, 2023
AuthorsEmile Dupuy / Sander Egbert Van der Verren / Jiusheng Lin / Mark Alan Wilson / Alix Vincent Dachsbeck / Felipe Viela / Emmanuelle Latour / Alexandra Gennaris / Didier Vertommen / Yves Frédéric Dufrêne / Bogdan Iuliu Iorga / Camille Véronique Goemans / Han Remaut / Jean-François Collet /
PubMed AbstractHsp60 chaperonins and their Hsp10 cofactors assist protein folding in all living cells, constituting the paradigmatic example of molecular chaperones. Despite extensive investigations of their ...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.
External linksCell / PubMed:36764293 / PubMed Central
MethodsEM (single particle)
Resolution3.4 Å
Structure data

14352

7ywy

EMDB-14352, PDB-7ywy:
Structure of the GroEL chaperonin in complex with the CnoX chaperedoxin
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • escherichia coli (E. coli)
KeywordsCHAPERONE / Protein Folding / Redox / Complex / Chaperonin

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