Autorepression of yeast Hsp70 cochaperones by intramolecular interactions involving their J-domains.

Détails

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Etat: Public
Version: Final published version
Licence: CC BY-NC-ND 4.0
ID Serval
serval:BIB_F1DAA741A6AE
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Autorepression of yeast Hsp70 cochaperones by intramolecular interactions involving their J-domains.
Périodique
Cell stress & chaperones
Auteur⸱e⸱s
Rebeaud M.E., Tiwari S., Fauvet B., Mohr A., Goloubinoff P., De Los Rios P.
ISSN
1466-1268 (Electronic)
ISSN-L
1355-8145
Statut éditorial
Publié
Date de publication
04/2024
Peer-reviewed
Oui
Volume
29
Numéro
2
Pages
338-348
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: ppublish
Résumé
The 70 kDa heat shock protein (Hsp70) chaperones control protein homeostasis in all ATP-containing cellular compartments. J-domain proteins (JDPs) coevolved with Hsp70s to trigger ATP hydrolysis and catalytically upload various substrate polypeptides in need to be structurally modified by the chaperone. Here, we measured the protein disaggregation and refolding activities of the main yeast cytosolic Hsp70, Ssa1, in the presence of its most abundant JDPs, Sis1 and Ydj1, and two swap mutants, in which the J-domains have been interchanged. The observed differences by which the four constructs differently cooperate with Ssa1 and cooperate with each other, as well as their observed intrinsic ability to bind misfolded substrates and trigger Ssa1's ATPase, indicate the presence of yet uncharacterized intramolecular dynamic interactions between the J-domains and the remaining C-terminal segments of these proteins. Taken together, the data suggest an autoregulatory role to these intramolecular interactions within both type A and B JDPs, which might have evolved to reduce energy-costly ATPase cycles by the Ssa1-4 chaperones that are the most abundant Hsp70s in the yeast cytosol.
Mots-clé
Saccharomyces cerevisiae/metabolism, HSP40 Heat-Shock Proteins/metabolism, Saccharomyces cerevisiae Proteins/metabolism, Protein Binding, HSP70 Heat-Shock Proteins/metabolism, Molecular Chaperones/metabolism, Adenosine Triphosphatases/metabolism, Adenosine Triphosphate/metabolism, Autorepression, Coevolution, DNAJA, DNAJB, JDPs
Pubmed
Web of science
Open Access
Oui
Création de la notice
25/03/2024 14:45
Dernière modification de la notice
25/05/2024 6:13
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