Journal article
Prion propagation by Hsp40 molecular chaperones
Prion, Vol.3(2), pp.59-64
04/2009
DOI: 10.4161/pri.3.2.9062
PMCID: PMC2712600
PMID: 19535913
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.
Details
- Title: Subtitle
- Prion propagation by Hsp40 molecular chaperones
- Creators
- Daniel W Summers - Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7090, USAPeter M DouglasDouglas M Cyr
- Resource Type
- Journal article
- Publication Details
- Prion, Vol.3(2), pp.59-64
- Publisher
- United States
- DOI
- 10.4161/pri.3.2.9062
- PMID
- 19535913
- PMCID
- PMC2712600
- ISSN
- 1933-6896
- eISSN
- 1933-690X
- Grant note
- 5T32GM008581-09 / NIGMS NIH HHS T32 GM008581 / NIGMS NIH HHS 5R01GM067785-06 / NIGMS NIH HHS R01 GM067785 / NIGMS NIH HHS
- Language
- English
- Date published
- 04/2009
- Academic Unit
- Iowa Neuroscience Institute; Biology
- Record Identifier
- 9984071688902771
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