Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress
Copyright © 2017 The Author(s). Published by Elsevier Inc. All rights reserved..
Self-perpetuating ordered protein aggregates (amyloids and prions) are associated with a variety of neurodegenerative disorders. Although environmental agents have been linked to certain amyloid diseases, the molecular basis of their action remains unclear. We have employed endogenous yeast prions as a model system to study environmental control of amyloid formation. A short-lived actin-associated yeast protein Lsb2 can trigger prion formation by other proteins in a mode regulated by the cytoskeleton and ubiquitin-dependent processes. Here, we show that such a heterologous prion induction is due to the ability of Lsb2 to form a transient prion state, generated in response to thermal stress. Evolutionary acquisition of prion-inducing activity by Lsb2 is traced to a single amino acid change, coinciding with the acquisition of thermotolerance in the Saccharomyces yeast lineage. This raises the intriguing possibility that the transient prion formation could aid in functioning of Lsb2 at higher temperatures.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2017 |
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| Erschienen: |
2017 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:18 |
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| Enthalten in: |
Cell reports - 18(2017), 3 vom: 17. Jan., Seite 751-761 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Chernova, Tatiana A [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 13.12.2017 Date Revised 13.11.2018 published: Print Citation Status MEDLINE |
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| doi: |
10.1016/j.celrep.2016.12.082 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 520 | |a Copyright © 2017 The Author(s). Published by Elsevier Inc. All rights reserved. | ||
| 520 | |a Self-perpetuating ordered protein aggregates (amyloids and prions) are associated with a variety of neurodegenerative disorders. Although environmental agents have been linked to certain amyloid diseases, the molecular basis of their action remains unclear. We have employed endogenous yeast prions as a model system to study environmental control of amyloid formation. A short-lived actin-associated yeast protein Lsb2 can trigger prion formation by other proteins in a mode regulated by the cytoskeleton and ubiquitin-dependent processes. Here, we show that such a heterologous prion induction is due to the ability of Lsb2 to form a transient prion state, generated in response to thermal stress. Evolutionary acquisition of prion-inducing activity by Lsb2 is traced to a single amino acid change, coinciding with the acquisition of thermotolerance in the Saccharomyces yeast lineage. This raises the intriguing possibility that the transient prion formation could aid in functioning of Lsb2 at higher temperatures | ||
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| 700 | 1 | |a Kiktev, Denis A |e verfasserin |4 aut | |
| 700 | 1 | |a Romanyuk, Andrey V |e verfasserin |4 aut | |
| 700 | 1 | |a Shanks, John R |e verfasserin |4 aut | |
| 700 | 1 | |a Laur, Oskar |e verfasserin |4 aut | |
| 700 | 1 | |a Ali, Moiez |e verfasserin |4 aut | |
| 700 | 1 | |a Ghosh, Abheek |e verfasserin |4 aut | |
| 700 | 1 | |a Kim, Dami |e verfasserin |4 aut | |
| 700 | 1 | |a Yang, Zhen |e verfasserin |4 aut | |
| 700 | 1 | |a Mang, Maggie |e verfasserin |4 aut | |
| 700 | 1 | |a Chernoff, Yury O |e verfasserin |4 aut | |
| 700 | 1 | |a Wilkinson, Keith D |e verfasserin |4 aut | |
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