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- W2059373914 startingPage "59" @default.
- W2059373914 abstract "Molecular chaperones regulate essential steps in the propagation of yeast prions. Yeast prions possess domains enriched in glutamines and asparagines that act as templates to drive the assembly of native proteins into beta-sheet-rich, amyloid-like fibrils. Several recent studies highlight a significant and complex function for Hsp40 co-chaperones in propagation of prion elements in yeast. Hsp40 co-chaperones bind non-native polypeptides and transfer these clients to Hsp70s for refolding or degradation. How Hsp40 co-chaperones bind amyloid-like prion conformers that are enriched in hydrophilic residues such as glutamines and asparagines is a significant question in the field. Interestingly, selective recognition of amyloid-like conformers by distinct Hsp40s appears to confer opposing actions on prion assembly. For example, the Type I Hsp40 Ydj1 and Type II Hsp40 Sis1 bind different regions within the prion protein Rnq1 and function respectively to inhibit or promote [RNQ+] prion assembly. Thus, substrate selectivity enables distinct Hsp40s to act at unique steps in prion propagation." @default.
- W2059373914 created "2016-06-24" @default.
- W2059373914 creator A5030361320 @default.
- W2059373914 creator A5033083330 @default.
- W2059373914 creator A5037467146 @default.
- W2059373914 date "2009-04-01" @default.
- W2059373914 modified "2023-09-26" @default.
- W2059373914 title "Prion propagation by Hsp40 molecular chaperones" @default.
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- W2059373914 doi "https://doi.org/10.4161/pri.3.2.9062" @default.
- W2059373914 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2712600" @default.
- W2059373914 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19535913" @default.
- W2059373914 hasPublicationYear "2009" @default.