Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones.

Détails

ID Serval
serval:BIB_6E5BA4791F9D
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones.
Périodique
Journal of Biological Chemistry
Auteur(s)
Ben-Zvi A.P., Goloubinoff P.
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Statut éditorial
Publié
Date de publication
2002
Peer-reviewed
Oui
Volume
277
Numéro
51
Pages
49422-49427
Langue
anglais
Résumé
External stresses or mutations may cause labile proteins to lose their distinct native conformations and seek alternatively stable aggregated forms. Molecular chaperones that specifically act on protein aggregates were used here as a tool to address the biochemical nature of stable homo- and hetero-aggregates from non-pathogenic proteins formed by heat-stress. Confirmed by sedimentation and activity measurements, chaperones demonstrated that a single polypeptide chain can form different species of aggregates, depending on the denaturing conditions. Indicative of a cascade reaction, sub-stoichiometric amounts of one fast-aggregating protein strongly accelerated the conversion of another soluble, slow-aggregating protein into insoluble, chaperone-resistant aggregates. Chaperones strongly inhibited seed-induced protein aggregation, suggesting that they can prevent and cure proteinaceous infectious behavior in homo- and hetero-aggregates from common and disease-associated proteins in the cell.
Mots-clé
Animals, Catalysis, Cattle, Centrifugation, Dimerization, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Escherichia coli Proteins/metabolism, Glucosephosphate Dehydrogenase/chemistry, Glucosephosphate Dehydrogenase/metabolism, Heat-Shock Proteins/metabolism, Malate Dehydrogenase/chemistry, Malate Dehydrogenase/metabolism, Molecular Chaperones/metabolism, Peptides/chemistry, Protein Binding, Protein Conformation, Rabbits, Serum Albumin, Bovine/chemistry, Serum Albumin, Bovine/metabolism, Spectrometry, Fluorescence, Subcellular Fractions, Swine, Temperature, Time Factors
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 21:02
Dernière modification de la notice
20/08/2019 15:27
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