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TitleHeritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 109, Issue 37, Page 14906-14911, Year 2012
Publish dateSep 11, 2012
AuthorsHelen R Saibil / Anja Seybert / Anja Habermann / Juliane Winkler / Mikhail Eltsov / Mario Perkovic / Daniel Castaño-Diez / Margot P Scheffer / Uta Haselmann / Petr Chlanda / Susan Lindquist / Jens Tyedmers / Achilleas S Frangakis /
PubMed AbstractYeast prions constitute a "protein-only" mechanism of inheritance that is widely deployed by wild yeast to create diverse phenotypes. One of the best-characterized prions, [PSI(+)], is governed by a ...Yeast prions constitute a "protein-only" mechanism of inheritance that is widely deployed by wild yeast to create diverse phenotypes. One of the best-characterized prions, [PSI(+)], is governed by a conformational change in the prion domain of Sup35, a translation-termination factor. When this domain switches from its normal soluble form to an insoluble amyloid, the ensuing change in protein synthesis creates new traits. Two factors make these traits heritable: (i) the amyloid conformation is self-templating; and (ii) the protein-remodeling factor heat-shock protein (Hsp)104 (acting together with Hsp70 chaperones) partitions the template to daughter cells with high fidelity. Prions formed by several other yeast proteins create their own phenotypes but share the same mechanistic basis of inheritance. Except for the amyloid fibril itself, the cellular architecture underlying these protein-based elements of inheritance is unknown. To study the 3D arrangement of prion assemblies in their cellular context, we examined yeast [PSI(+)] prions in the native, hydrated state in situ, taking advantage of recently developed methods for cryosectioning of vitrified cells. Cryo-electron tomography of the vitrified sections revealed the prion assemblies as aligned bundles of regularly spaced fibrils in the cytoplasm with no bounding structures. Although the fibers were widely spaced, other cellular complexes, such as ribosomes, were excluded from the fibril arrays. Subtomogram image averaging, made possible by the organized nature of the assemblies, uncovered the presence of an additional array of densities between the fibers. We suggest these structures constitute a self-organizing mechanism that coordinates fiber deposition and the regulation of prion inheritance.
External linksProc Natl Acad Sci U S A / PubMed:22927413 / PubMed Central
MethodsEM (subtomogram averaging)
Structure data

EMDB-2103:
Heritable yeast prions have a highly organized 3-dimensional architecture with inter-fiber structures
Method: EM (subtomogram averaging)

EMDB-2104:
Heritable yeast prions have a highly organized 3-dimensional architecture with inter-fiber structures
Method: EM (subtomogram averaging)

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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