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| Content Provider | PubMed Central |
|---|---|
| Author | Derkatch, I. L. Bradley, M. E. Zhou, P. Chernoff, Y. O. Liebman, S. W. |
| Abstract | It has previously been shown that yeast prion [PSI(+)] is cured by GuHCl, although reports on reversibility of curing were contradictory. Here we show that GuHCl treatment of both [PSI(+)] and [psi(-)] yeast strains results in two classes of [psi(-)] derivatives: Pin(+), in which [PSI(+)] can be reinduced by Sup35p overproduction, and Pin(-), in which overexpression of the complete SUP35 gene does not lead to the [PSI(+)] appearance. However, in both Pin(+) and Pin(-) derivatives [PSI(+)] is reinduced by overproduction of a short Sup35p N-terminal fragment, thus, in principle, [PSI(+)] curing remains reversible in both cases. Neither suppression nor growth inhibition caused by SUP35 overexpression in Pin(+) [psi(-)] derivatives are observed in Pin(-) [psi(-)] derivatives. Genetic analyses show that the Pin(+) phenotype is determined by a non-Mendelian factor, which, unlike the [PSI(+)] prion, is independent of the Sup35p N-terminal domain. A Pin(-) [psi(-)] derivative was also generated by transient inactivation of the heat shock protein, Hsp104, while [PSI(+)] curing by Hsp104 overproduction resulted exclusively in Pin(+) [psi(-)] derivatives. We hypothesize that in addition to the [PSI(+)] prion-determining domain in the Sup35p N-terminus, there is another self-propagating conformational determinant in the C-proximal part of Sup35p and that this second prion is responsible for the Pin(+) phenotype. |
| Starting Page | 507 |
| File Format | |
| ISSN | 00166731 |
| Journal | Genetics |
| Issue Number | 2 |
| Volume Number | 147 |
| Language | English |
| Publisher Date | 1997-10-01 |
| Access Restriction | Open |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics |
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