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Article

The role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variants.

Genetics - 1 Feb 2006

Shkundina Irina S, Kushnirov Vitaly V, Tuite Mick F, Ter-Avanesyan Michael D

Abstract excerpt

The cytoplasmic [PSI+] determinant of Saccharomyces cerevisiae is the prion form of the Sup35 protein. Oligopeptide repeats within the Sup35 N-terminal domain (PrD) presumably are required for the stable [PSI+] inheritance that in turn involves fragmentation of Sup35 polymers by the chaperone Hsp104. The nonsense suppressor [PSI+] phenotype can vary in efficiency probably due to different inheritable Sup35...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 16272413
DOI: 10.1534/genetics.105.048660
PMCID: PMC1456247

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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The role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variants.PMID 16272413Read ↗

The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+] prions.Semantic proximity Read ↗

Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor.Semantic proximity Read ↗

Effect of charged residues in the N-domain of Sup35 protein on prion [PSI+] stability and propagation.Semantic proximity Read ↗

The PNM2 mutation in the prion protein domain of SUP35 has distinct effects on different variants of the [PSI+] prion in yeast.Semantic proximity Read ↗

Supporting the structural basis of prion strains: induction and identification of [PSI] variants.Semantic proximity Read ↗

Structural definition is important for the propagation of the yeast [PSI+] prion.Semantic proximity Read ↗

Conformation preserved in a weak-to-strong or strong-to-weak [PSI+] conversion during transmission to Sup35 prion variants.Semantic proximity Read ↗

The [PSI+] prion of yeast: a problem of inheritance.Semantic proximity Read ↗

[Modification of [PSI+] prion properties by the combination of amino acid changes within Sup35 protein N-domain].Semantic proximity Read ↗

Importance of the Hsp70 ATPase domain in yeast prion propagation.Semantic proximity Read ↗

Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversion.Semantic proximity Read ↗

In vitro propagation of the prion-like state of yeast Sup35 protein.Semantic proximity Read ↗

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