Mechanism of inhibition of Psi+ prion determinant propagation by a mutation of the N-terminus of the yeast Sup35 protein

Asp change in the Sup35p N-terminal domain eliminates Psi+. Here we observed that the mutant Sup35p can be converted to the prion-like form in vitro, but such conversion proceeds slower than that of wild-type Sup35p. The overexpression of mutant Sup35p induced the de novo appearance of Psi+ cells containing the prion-like form of mutant Sup35p, which was able to transmit its properties to wild-type Sup35p both in vitro and in vivo. Our data indicate that this Psi+-eliminating mutation does not alter the initial binding of Sup35p molecules to the Sup35p Psi+-specific aggregates, but rather inhibits its subsequent prion-like rearrangement and/or binding of the next Sup35p molecule to the growing prion-like Sup35p aggregate. -->

ISSN:	0261-4189
Přístupová URL adresa:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e822d9415792dd88b002e6df24bdfe52 https://pubmed.ncbi.nlm.nih.gov/9755180
Rights:	OPEN
Přírůstkové číslo:	edsair.doi.dedup.....e822d9415792dd88b002e6df24bdfe52
Autor:	Sergey Paushkin, Michael D. Ter-Avanesyan, Mick F. Tuite, Vitaly V. Kushnirov, Brian S. Cox, Natalia V. Kochneva-Pervukhova
Rok vydání:	1998
Předmět:	Saccharomyces cerevisiae Proteins Prions Saccharomyces cerevisiae Mutant Gene Dosage medicine.disease_cause General Biochemistry Genetics and Molecular Biology Fungal Proteins medicine Molecular Biology Gene Mutation Fungal protein General Immunology and Microbiology biology General Neuroscience biology.organism_classification Molecular biology In vitro Cell biology N-terminus Chromosomes Fungal Release factor Peptide Termination Factors Research Article
Zdroj:	The EMBO journal. 17(19)
ISSN:	0261-4189
Popis:	The SUP35 gene of Saccharomyces cerevisiae encodes the polypeptide chain release factor eRF3. This protein (also called Sup35p) is thought to be able to undergo a heritable conformational switch, similarly to mammalian prions, giving rise to the cytoplasmically inherited Psi+ determinant. A dominant mutation (PNM2 allele) in the SUP35 gene causing a Gly58-->Asp change in the Sup35p N-terminal domain eliminates Psi+. Here we observed that the mutant Sup35p can be converted to the prion-like form in vitro, but such conversion proceeds slower than that of wild-type Sup35p. The overexpression of mutant Sup35p induced the de novo appearance of Psi+ cells containing the prion-like form of mutant Sup35p, which was able to transmit its properties to wild-type Sup35p both in vitro and in vivo. Our data indicate that this Psi+-eliminating mutation does not alter the initial binding of Sup35p molecules to the Sup35p Psi+-specific aggregates, but rather inhibits its subsequent prion-like rearrangement and/or binding of the next Sup35p molecule to the growing prion-like Sup35p aggregate.
Databáze:	OpenAIRE
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