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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | O'driscoll, Jonathan Clare, Daniel Saibil, Helen |
| Description | Author Affiliation: O'Driscoll J ( Crystallography, Department of Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, UK.); Clare D ( Crystallography, Department of Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, UK.); Saibil H ( Crystallography, Department of Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, UK h.saibil@mail.cryst.bbk.ac.uk.) |
| Abstract | Prions consist of misfolded proteins that have adopted an infectious amyloid conformation. In vivo, prion biogenesis is intimately associated with the protein quality control machinery. Using electron tomography, we probed the effects of the heat shock protein Hsp70 chaperone system on the structure of a model yeast [PSI+] prion in situ. Individual Hsp70 deletions shift the balance between fibril assembly and disassembly, resulting in a variable shell of nonfibrillar, but still immobile, aggregates at the surface of the [PSI+] prion deposits. Both Hsp104 (an Hsp100 disaggregase) and Sse1 (the major yeast form of Hsp110) were localized to this surface shell of [PSI+] deposits in the deletion mutants. Elevation of Hsp104 expression promoted the appearance of this novel, nonfibrillar form of the prion aggregate. Moreover, Sse1 was found to regulate prion fibril length. Our studies reveal a key role for Sse1 (Hsp110), in cooperation with Hsp104, in regulating the length and assembly state of [PSI+] prion fibrils in vivo. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 1 |
| Volume Number | 211 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2015-10-12 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Heat-Shock Proteins Metabolism Prions Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Enzymology HSP110 Heat-Shock Proteins HSP70 Heat-Shock Proteins Ultrastructure Protein Aggregates Research Support, Non-U.S. Gov't Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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