Unknown

Dataset Information

0

The [PSI +] yeast prion does not wildly affect proteome composition whereas selective pressure exerted on [PSI +] cells can promote aneuploidy.


ABSTRACT: The yeast Sup35 protein is a subunit of the translation termination factor, and its conversion to the [PSI +] prion state leads to more translational read-through. Although extensive studies have been done on [PSI +], changes at the proteomic level have not been performed exhaustively. We therefore used a SILAC-based quantitative mass spectrometry approach and identified 4187 proteins from both [psi -] and [PSI +] strains. Surprisingly, there was very little difference between the two proteomes under standard growth conditions. We found however that several [PSI +] strains harbored an additional chromosome, such as chromosome I. Albeit, we found no evidence to support that [PSI +] induces chromosomal instability (CIN). Instead we hypothesized that the selective pressure applied during the establishment of [PSI +]-containing strains could lead to a supernumerary chromosome due to the presence of the ade1-14 selective marker for translational read-through. We therefore verified that there was no prevalence of disomy among newly generated [PSI +] strains in absence of strong selection pressure. We also noticed that low amounts of adenine in media could lead to higher levels of mitochondrial DNA in [PSI +] in ade1-14 cells. Our study has important significance for the establishment and manipulation of yeast strains with the Sup35 prion.

SUBMITTER: Chan PHW 

PROVIDER: S-EPMC5559586 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

The [PSI <sup>+</sup>] yeast prion does not wildly affect proteome composition whereas selective pressure exerted on [PSI <sup>+</sup>] cells can promote aneuploidy.

Chan Patrick H W PHW   Lee Lisa L   Kim Erin E   Hui Tony T   Stoynov Nikolay N   Nassar Roy R   Moksa Michelle M   Cameron Dale M DM   Hirst Martin M   Gsponer Joerg J   Mayor Thibault T  

Scientific reports 20170816 1


The yeast Sup35 protein is a subunit of the translation termination factor, and its conversion to the [PSI <sup>+</sup>] prion state leads to more translational read-through. Although extensive studies have been done on [PSI <sup>+</sup>], changes at the proteomic level have not been performed exhaustively. We therefore used a SILAC-based quantitative mass spectrometry approach and identified 4187 proteins from both [psi <sup>-</sup>] and [PSI <sup>+</sup>] strains. Surprisingly, there was very  ...[more]

Similar Datasets

| S-EPMC7084296 | biostudies-literature
| S-EPMC3543502 | biostudies-literature
| S-EPMC3069153 | biostudies-other
| S-EPMC2533192 | biostudies-literature
| S-EPMC3679450 | biostudies-literature
| S-EPMC7274466 | biostudies-literature
| S-EPMC2669030 | biostudies-literature
| S-EPMC2650407 | biostudies-literature
| S-EPMC5599042 | biostudies-literature
| S-EPMC2978756 | biostudies-literature