Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism.

The EMBO journal - 1 Apr 1999

Eaglestone S S, Cox B S, Tuite M F

Abstract excerpt

[PSI+] is a protein-based heritable phenotype of the yeast Saccharomyces cerevisiae which reflects the prion-like behaviour of the endogenous Sup35p protein release factor. [PSI+] strains exhibit a marked decrease in translation termination efficiency, which permits decoding of translation termination signals and, presumably, the production of abnormally extended polypeptides. We have examined whether the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Fungal Proteins
Share to Genes, Fungal
Share to Hot Temperature

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Peptide Termination Factors

Share to Prions

Share to Protein Biosynthesis

Share to Saccharomyces cerevisiae Proteins

Share to Suppression, Genetic

Source

Open in PubMed Open full text

Identifiers

PMID: 10202160
DOI: 10.1093/emboj/18.7.1974
PMCID: PMC1171282

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism.PMID 10202160Read ↗

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

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

Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits.Semantic proximity Read ↗

A prolonged chronological lifespan is an unexpected benefit of the [PSI+] prion in yeast.Semantic proximity Read ↗

Assessment of inactivating stop codon mutations in forty Saccharomyces cerevisiae strains: implications for [PSI] prion- mediated phenotypes.Semantic proximity Read ↗

The [PSI+] prion exists as a dynamic cloud of variants.Semantic proximity Read ↗

Detection system- and strain-dependent diversity of de novo [PSI+] prion generation and phenotypes in Saccharomyces cerevisiae.Semantic proximity Read ↗

Mutants of the Paf1 complex alter phenotypic expression of the yeast prion [PSI+].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 ↗

Increased -1 ribosomal frameshifting efficiency by yeast prion-like phenotype [PSI+].Semantic proximity Read ↗

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

A yeast prion provides a mechanism for genetic variation and phenotypic diversity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.