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Verfasst von:Tyedmers, Jens [VerfasserIn]   i
 Treusch, Sebastian [VerfasserIn]   i
 Dong, Jijun [VerfasserIn]   i
 McCaffery, J. Michael [VerfasserIn]   i
 Bevis, Brooke [VerfasserIn]   i
 Lindquist, Susan [VerfasserIn]   i
Titel:Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation
Verf.angabe:Jens Tyedmers, Sebastian Treusch, Jijun Dong, J. Michael McCaffery, Brooke Bevis, and Susan Lindquist
E-Jahr:2010
Jahr:April 26, 2010
Umfang:6 S.
Fussnoten:Gesehen am 26.01.2024
Titel Quelle:Enthalten in: National Academy of Sciences (Washington, DC)Proceedings of the National Academy of Sciences of the United States of America
Ort Quelle:Washington, DC : National Acad. of Sciences, 1915
Jahr Quelle:2010
Band/Heft Quelle:107(2010), 19, Seite 8633-8638
ISSN Quelle:1091-6490
Abstract:When the translation termination factor Sup35 adopts the prion state, [PSI+], the read-through of stop codons increases, uncovering hidden genetic variation and giving rise to new, often beneficial, phenotypes. Evidence suggests that prion induction involves a process of maturation, but this has never been studied in detail. To do so, we used a visually tractable prion model consisting of the Sup35 prion domain fused to GFP (PrD-GFP) and overexpressed it to achieve induction in many cells simultaneously. PrD-GFP first assembled into Rings as previously described. Rings propagated for many generations before the protein transitioned into a Dot structure. Dots transmitted the [PSI+] phenotype through mating and meiosis, but Rings did not. Surprisingly, the underlying amyloid conformation of PrD-GFP was identical in Rings and Dots. However, by electron microscopy, Rings consisted of very long uninterrupted bundles of fibers, whereas Dot fibers were highly fragmented. Both forms were deposited at the IPOD, a biologically ancient compartment for the deposition of irreversibly aggregated proteins that we propose is the site of de novo prion induction. We find that oxidatively damaged proteins are also localized there, helping to explain how proteotoxic stresses increase the rate of prion induction. Curing PrD-GFP prions, by inhibiting Hsp104’s fragmentation activity, reversed the induction process: Dot cells produced Rings before PrD-GFP reverted to the soluble state. Thus, formation of the genetically transmissible prion state is a two-step process that involves an ancient system for the asymmetric inheritance of damaged proteins and heritable changes in the extent of prion fragmentation.
DOI:doi:10.1073/pnas.1003895107
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: https://doi.org/10.1073/pnas.1003895107
 Volltext: https://www.pnas.org/doi/full/10.1073/pnas.1003895107
 DOI: https://doi.org/10.1073/pnas.1003895107
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1879068087
Verknüpfungen:→ Zeitschrift

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