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

Details

Serval ID
serval:BIB_6E5BA4791F9D
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones.
Journal
Journal of Biological Chemistry
Author(s)
Ben-Zvi A.P., Goloubinoff P.
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Publication state
Published
Issued date
2002
Peer-reviewed
Oui
Volume
277
Number
51
Pages
49422-49427
Language
english
Abstract
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.
Keywords
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
Yes
Create date
24/01/2008 20:02
Last modification date
20/08/2019 14:27
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