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Article

Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation.

Molecular and cellular biology - 1 May 1997

Paushkin S V, Kushnirov V V, Smirnov V N, Ter-Avanesyan M D

Abstract excerpt

The SUP45 and SUP35 genes of Saccharomyces cerevisiae encode polypeptide chain release factors eRF1 and eRF3, respectively. It has been suggested that the Sup35 protein (Sup35p) is subject to a heritable conformational switch, similar to mammalian prions, thus giving rise to the non-Mendelian [PS...

Topics

Electrophoresis, Polyacrylamide Gel
Endopeptidases
Fungal Proteins
Heat-Shock Proteins
Molecular Weight
Peptide Termination Factors
Phenotype
Prions
Protein Biosynthesis
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins

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Identifiers

PMID: 9111351
DOI: 10.1128/MCB.17.5.2798
PMCID: PMC232131

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9111351-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation.PMID 9111351Read ↗

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

Mechanism of inhibition of Psi+ prion determinant propagation by a mutation of the N-terminus of the yeast Sup35 protein.Semantic proximity Read ↗

Nonsense Mutations in the Yeast SUP35 Gene Affect the [PSI+] Prion Propagation.Semantic proximity Read ↗

[Fusion of glutathione S-transferase with the N-terminus of yeast Sup35p protein inhibits its prion-like properties].Semantic proximity Read ↗

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

The yeast non-Mendelian factor [ETA+] is a variant of [PSI+], a prion-like form of release factor eRF3.Semantic proximity Read ↗

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

SFP1-mediated prion-dependent lethality is caused by increased Sup35 aggregation and alleviated by Sis1.Semantic proximity Read ↗

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

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Epigenetic control of polyamines by the prion [PSI+].Semantic proximity Read ↗

C-terminal truncation of the Sup35 protein increases the frequency of de novo generation of a prion-based [PSI+] determinant in Saccharomyces cerevisiae.Semantic proximity Read ↗

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