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 t...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Patrick H. W. Chan, Lisa Lee, Erin Kim, Tony Hui, Nikolay Stoynov, Roy Nassar, Michelle Moksa, Dale M. Cameron, Martin Hirst, Joerg Gsponer, Thibault Mayor
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a569e4de8af44e818ecb8e5ecd751652
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:a569e4de8af44e818ecb8e5ecd751652
record_format	dspace
spelling	oai:doaj.org-article:a569e4de8af44e818ecb8e5ecd7516522021-12-02T12:30:35ZThe [PSI +] yeast prion does not wildly affect proteome composition whereas selective pressure exerted on [PSI +] cells can promote aneuploidy10.1038/s41598-017-07999-82045-2322https://doaj.org/article/a569e4de8af44e818ecb8e5ecd7516522017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-07999-8https://doaj.org/toc/2045-2322Abstract 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.Patrick H. W. ChanLisa LeeErin KimTony HuiNikolay StoynovRoy NassarMichelle MoksaDale M. CameronMartin HirstJoerg GsponerThibault MayorNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-15 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Patrick H. W. Chan Lisa Lee Erin Kim Tony Hui Nikolay Stoynov Roy Nassar Michelle Moksa Dale M. Cameron Martin Hirst Joerg Gsponer Thibault Mayor The [PSI +] yeast prion does not wildly affect proteome composition whereas selective pressure exerted on [PSI +] cells can promote aneuploidy
description	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.
format	article
author	Patrick H. W. Chan Lisa Lee Erin Kim Tony Hui Nikolay Stoynov Roy Nassar Michelle Moksa Dale M. Cameron Martin Hirst Joerg Gsponer Thibault Mayor
author_facet	Patrick H. W. Chan Lisa Lee Erin Kim Tony Hui Nikolay Stoynov Roy Nassar Michelle Moksa Dale M. Cameron Martin Hirst Joerg Gsponer Thibault Mayor
author_sort	Patrick H. W. Chan
title	The [PSI +] yeast prion does not wildly affect proteome composition whereas selective pressure exerted on [PSI +] cells can promote aneuploidy
title_short	The [PSI +] yeast prion does not wildly affect proteome composition whereas selective pressure exerted on [PSI +] cells can promote aneuploidy
title_full	The [PSI +] yeast prion does not wildly affect proteome composition whereas selective pressure exerted on [PSI +] cells can promote aneuploidy
title_fullStr	The [PSI +] yeast prion does not wildly affect proteome composition whereas selective pressure exerted on [PSI +] cells can promote aneuploidy
title_full_unstemmed	The [PSI +] yeast prion does not wildly affect proteome composition whereas selective pressure exerted on [PSI +] cells can promote aneuploidy
title_sort	[psi +] yeast prion does not wildly affect proteome composition whereas selective pressure exerted on [psi +] cells can promote aneuploidy
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/a569e4de8af44e818ecb8e5ecd751652
work_keys_str_mv	AT patrickhwchan thepsiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT lisalee thepsiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT erinkim thepsiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT tonyhui thepsiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT nikolaystoynov thepsiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT roynassar thepsiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT michellemoksa thepsiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT dalemcameron thepsiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT martinhirst thepsiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT joerggsponer thepsiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT thibaultmayor thepsiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT patrickhwchan psiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT lisalee psiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT erinkim psiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT tonyhui psiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT nikolaystoynov psiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT roynassar psiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT michellemoksa psiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT dalemcameron psiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT martinhirst psiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT joerggsponer psiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy AT thibaultmayor psiyeastpriondoesnotwildlyaffectproteomecompositionwhereasselectivepressureexertedonpsicellscanpromoteaneuploidy
_version_	1718394353622188032

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

Ejemplares similares