Kochneva-Pervukhova, N.V. and Paushkin, S.V. and Kushnirov, V.V. and Cox, B.S. and Tuite, M.F. and Ter-Avanesyan, M.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.
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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: | 04 Apr 2009 18:19 |
| Resource URI: | http://kar.kent.ac.uk/id/eprint/17404 (The current URI for this page, for reference purposes) |
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