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

Kochneva-Pervukhova, Natalia V. and Paushkin, Sergey V. and Kushnirov, Vitaly V. and Cox, Brian S. and Tuite, Mick F. and Ter-Avanesyan, Michael D. (1998) Mechanism of inhibition of Psi(+) prion determinant propagation by a mutation of the N-terminus of the yeast Sup35 protein. Embo Journal, 17 (19). pp. 5805-5810. ISSN 0261-4189. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1093/emboj/17.19.5805

Abstract

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 Y+. 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.

Item Type: Article
Uncontrolled keywords: prion; release factor eRF3; Saccharomyces cerevisiae; translation termination
Subjects: Q Science > Q Science (General)
Q Science > QH Natural history
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: M.A. Ziai
Date Deposited: 04 Apr 2009 18:19
Last Modified: 10 Jun 2014 12:47
Resource URI: http://kar.kent.ac.uk/id/eprint/17404 (The current URI for this page, for reference purposes)
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