Eaglestone, Simon S. and Cox, Brian S. and Tuite, Mick F. (1999) Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism. Embo Journal, 18 (7). pp. 1974-1981. ISSN 0261-4189. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
[PSI+] is a protein-based heritable phenotype of the yeast Saccharomyces cerevisiae which reflects the prion-like behaviour of the endogenous Sup35p protein release factor. [PSI+] strains exhibit a marked decrease in translation termination efficiency, which permits decoding of translation termination signals and, presumably, the production of abnormally extended polypeptides. We have examined whether the [PSI+]-induced expression of such an altered proteome might confer some selective growth advantage over [psi(-)] strains. Although otherwise isogenic [PSI+] and [psi(-)] strains show no difference in growth rates under normal laboratory conditions, we demonstrate that [PSI+] strains do exhibit enhanced tolerance to heat and chemical stress, compared with [psi(-)] strains. Moreover, we also show that the prion-like determinant [PSI+] is able to regulate translation termination efficiency in response to environmental stress, since growth in the presence of ethanol results in a transient increase in the efficiency of translation termination and a loss of the [PSI+] phenotype. We present a model to describe the prion-mediated regulation of translation termination efficiency and discuss its implications in relation to the potential physiological role of prions in S. cerevisiae and other fungi.
|Uncontrolled keywords:||environmental stress; phenotype; prion; yeast (Saccharomyces cerevisiae)|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||M. Nasiriavanaki|
|Date Deposited:||21 Jun 2009 11:00|
|Last Modified:||10 Jun 2014 12:45|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/17309 (The current URI for this page, for reference purposes)|