Molecular basis of a yeast prion species barrier

Article Abstract:

Molecular basis of a yeast prion species boundary is discussed. Sup35p from a spectrum of Saccharomycetales, bedding yeasts, has been cloned and characterized. Ability to support a prion inheritance mechanism was found to be conserved widely.

Usage, Evolution (Biology), Cytochemistry, Cladistic analysis, Origin of species

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Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(sup)+] prion

Article Abstract:

Research shows that the yeast prion [PSI(sup)+] is induced from gain-of-function properties of New1p and Rnq1p aggregates. The Gln/Asn-rich prion domains of these proteins control the susceptibility of [PSI(sup)+] induction and aggregation of human glutamine expansion disease protein.

Protein synthesis, Protein biosynthesis, Epigenesis

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A critical role for amino-terminal glutamine/aspargine repeats in the formation and propagation of a yeast prion

Article Abstract:

The Saccharomyces cerevisiae [PSI+] factor is a non-Mendelian trait that causes suppression of nonsense mutations in the yeast. To elucidate the conversion of amyloid fibril from its native state, the prion-like mechanism behind the propagation of the [PSI+] factor was investigated. The [PSI+] system was used to define sequence requirements for the in vivo formation and propagation of Sup35p amyloids. Results revealed a critical role for glutamine and asparagine residues in the amyloid state's stability. In addition, insights were made about the prion hypothesis.

Gene mutations, Gene mutation, Proteins

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