Impact of Amyloid Polymorphism on Prion-Chaperone Interactions in Yeast
| العنوان: | Impact of Amyloid Polymorphism on Prion-Chaperone Interactions in Yeast |
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| المؤلفون: | Justin K. Hines, Sarah C. Miller, Andrea N. Killian |
| المصدر: | Viruses Viruses, Vol 11, Iss 4, p 349 (2019) |
| بيانات النشر: | MDPI AG, 2019. |
| سنة النشر: | 2019 |
| مصطلحات موضوعية: | Ydj1, 0301 basic medicine, Amyloid, Saccharomyces cerevisiae Proteins, Prions, Saccharomyces cerevisiae, lcsh:QR1-502, Swa2, Amyloidogenic Proteins, Review, Models, Biological, lcsh:Microbiology, 03 medical and health sciences, 0302 clinical medicine, Virology, Hdj1, Protein Interaction Domains and Motifs, Ssa, Ssb, biology, Sis1, Chemistry, biology.organism_classification, Phenotype, Hsp90, Apj1, Yeast, Hsp70, J-protein, 030104 developmental biology, Infectious Diseases, Biochemistry, Chaperone (protein), biology.protein, 030217 neurology & neurosurgery, Molecular Chaperones |
| الوصف: | Yeast prions are protein-based genetic elements found in the baker’s yeast Saccharomyces cerevisiae, most of which are amyloid aggregates that propagate by fragmentation and spreading of small, self-templating pieces called propagons. Fragmentation is carried out by molecular chaperones, specifically Hsp104, Hsp70, and Hsp40. Like other amyloid-forming proteins, amyloid-based yeast prions exhibit structural polymorphisms, termed “strains„ in mammalian systems and “variants„ in yeast, which demonstrate diverse phenotypes and chaperone requirements for propagation. Here, the known differential interactions between chaperone proteins and yeast prion variants are reviewed, specifically those of the yeast prions [PSI+], [RNQ+]/[PIN+], and [URE3]. For these prions, differences in variant-chaperone interactions (where known) with Hsp104, Hsp70s, Hsp40s, Sse1, and Hsp90 are summarized, as well as some interactions with chaperones of other species expressed in yeast. As amyloid structural differences greatly impact chaperone interactions, understanding and accounting for these variations may be crucial to the study of chaperones and both prion and non-prion amyloids. |
| تدمد: | 1999-4915 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff6eabc89dbaac1c0345acdfd10a4e33Test https://doi.org/10.3390/v11040349Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....ff6eabc89dbaac1c0345acdfd10a4e33 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 19994915 |
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