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

A G-protein gamma subunit mimic is a general antagonist of prion propagation in Saccharomyces cerevisiae.

Proceedings of the National Academy of Sciences of the United States of America - 20 Jan 2009

Ishiwata Masao, Kurahashi Hiroshi, Nakamura Yoshikazu

Abstract excerpt

The Gpg1 protein is a Ggamma subunit mimic implicated in the G-protein glucose-signaling pathway in Saccharomyces cerevisiae, and its function is largely unknown. Here we report that Gpg1 blocks the maintenance of [PSI(+)], an aggregated prion form of the translation termination factor Sup35. Although the GPG1 gene is normally not expressed, over-expression of GPG1 inhibits propagation of not only [PSI(+)] but...

Read the complete abstract on PubMed

Topics

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

Share to GTP-Binding Protein alpha Subunits
Share to GTP-Binding Protein beta Subunits

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to GTP-Binding Protein gamma Subunits

Share to Heat-Shock Proteins

Share to Mutation

Share to Prions

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 19129493
DOI: 10.1073/pnas.0808383106
PMCID: PMC2630093

Provenance

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A G-protein gamma subunit mimic is a general antagonist of prion propagation in Saccharomyces cerevisiae.PMID 19129493Read ↗

A heritable switch in carbon source utilization driven by an unusual yeast prion.Semantic proximity Read ↗

[PSI(+)] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast.Semantic proximity Read ↗

The protein-only theory and the yeast Saccharomyces cerevisiae: the prions and the propagons.Semantic proximity Read ↗

Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model.Semantic proximity Read ↗

Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation.Semantic proximity Read ↗

Guanidine reduces stop codon read-through caused by missense mutations in SUP35 or SUP45.Semantic proximity Read ↗

Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion.Semantic proximity Read ↗

The Candida albicans Sup35p protein (CaSup35p): function, prion-like behaviour and an associated polyglutamine length polymorphism.Semantic proximity Read ↗

Suppression of a dominant G-protein beta-subunit mutation in yeast by G alpha protein expression.Semantic proximity Read ↗

Protein Folding Activity of the Ribosome is involved in Yeast Prion Propagation.Semantic proximity Read ↗

Characterization of GPI14/YJR013w mutation that induces the cell wall integrity signalling pathway and results in increased protein production in Saccharomyces cerevisiae.Semantic proximity Read ↗

Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding.Semantic proximity Read ↗

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