Prion Variants of Yeast are Numerous, Mutable, and Segregate on Growth, Affecting Prion Pathogenesis, Transmission Barriers, and Sensitivity to Anti-Prion Systems

Autor: Reed B. Wickner, Moonil Son, Herman K. Edskes

Publikováno v: Viruses, Vol 11, Iss 3, p 238 (2019)

The known amyloid-based prions of Saccharomyces cerevisiae each have multiple heritable forms, called “prion variants” or “prion strains”. These variants, all based on the same prion protein sequence, differ in their biological properties and

Externí odkaz: https://doaj.org/article/c7977aae3a784068add319a03a7ade78

Point mutations affecting yeast prion propagation change the structure of its amyloid fibrils

Autor: Mikhail V. Belousov, Irina M. Kuznetsova, Nina P. Trubitsina, Anna I. Sulatskaya, Galina A. Zhouravleva, Maksim I. Sulatsky, Konstantin K. Turoverov, Manuel A. Llanos, Stanislav A. Bondarev, Andrey V. Kajava

Publikováno v: Journal of Molecular Liquids
Journal of Molecular Liquids, Elsevier, 2020, 314, pp.113618. ⟨10.1016/j.molliq.2020.113618⟩
SEDICI (UNLP)
Universidad Nacional de La Plata
instacron:UNLP

We investigated the effect of the point substitutions in the N-terminal domain of the yeast prion protein Sup35 (Sup35NMp) on the structure of its amyloid fibrils. As the objects of the study, proteins with mutations that have different influence on

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1efef5b42e593965472eb28d8ce04d82
https://doi.org/10.1016/j.molliq.2020.113618

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Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p

Autor: Ronald Melki, Birgit Habenstein, Anne K. Schütz, Nina Luckgei, Beat H. Meier, Anders B. Nielsen, Anja Böckmann, Luc Bousset, Yannick Sourigues

Publikováno v: Biomolecular NMR Assignments
Biomolecular NMR Assignments, Springer, 2014, 8 (2), pp.349-56. ⟨10.1007/s12104-013-9515-1⟩
Biomolecular NMR Assignments, 8 (2)
Biomolecular NMR assignments

Sup35p is a yeast prion and is responsible for the [PSI +] trait in Saccharomyces cerevisiae. With 685 amino acids, full-length soluble and fibrillar Sup35p are challenging targets for structural biology as they cannot be investigated by X-ray crysta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81d0ab0c55d1eb087883fa4cf8571cf5
https://hal.archives-ouvertes.fr/hal-01181115

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