Proteomics

Dataset Information

0

Proteomic analysis of [PSI+] yeast strain


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.

INSTRUMENT(S): Bruker Daltonics instrument model

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

TISSUE(S): Haploid

DISEASE(S): Disease Free

SUBMITTER: Patrick Hau Wing Chan  

LAB HEAD: Thibault Mayor

PROVIDER: PXD007168 | Pride | 2018-10-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
EditedProteinGroups.txt Txt
MSRawFiles.zip Other
OxidationMSites.txt Txt
allPeptides.txt Txt
evidence.txt Txt
Items per page:
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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]

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