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• W2046585102 abstract "The aggregation of the baker's yeast prion Sup35p is at the origin of the transmissible [PSI(+)] trait. We and others have shown that molecular chaperones modulate Sup35p aggregation. However, other protein classes might be involved in [PSI(+)] formation.We designed a functional proteomic study that combines two techniques to identify modulators of Sup35p aggregation and describe the changes associated to [PSI(+)] formation. The first allows measuring the effect of fractionated Saccharomyces cerevisiae cytosolic extracts from [PSI(+)] and [psi(-)] yeast cells on Sup35p assembly. The second is a multiplex qualitative and quantitative comparison of protein composition of active and inactive fractions using a gel-free and label-free LC-MS approach. We identify changes in proteins involved in translation, folding, degradation, oxido-reduction and metabolic processes.Our functional proteomic study provides the first inventory list of over 300 proteins that directly or indirectly affect Sup35p aggregation and [PSI(+)] formation. Our results highlight the complexity of the cellular changes accompanying [PSI(+)] formation and pave the way for in vitro studies aimed to document the effect of individual and/or combinations of proteins identified here, susceptible of affecting Sup35p assembly." @default.
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• W2046585102 date "2011-09-13" @default.
• W2046585102 modified "2023-09-24" @default.
• W2046585102 title "Qualitative and Quantitative Multiplexed Proteomic Analysis of Complex Yeast Protein Fractions That Modulate the Assembly of the Yeast Prion Sup35p" @default.
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• W2046585102 doi "https://doi.org/10.1371/journal.pone.0023659" @default.
• W2046585102 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3172207" @default.
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• W2046585102 hasPublicationYear "2011" @default.
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