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- Title
Qualitative and Quantitative Multiplexed Proteomic Analysis of Complex Yeast Protein Fractions That Modulate the Assembly of the Yeast Prion Sup35p.
- Authors
Redeker, Virginie; Hughes, Chris; Savistchenko, Jimmy; Vissers, Johannes P. C.; Melki, Ronald
- Abstract
Background: 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. Results: 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 labelfree LC-MS approach. We identify changes in proteins involved in translation, folding, degradation, oxido-eduction and metabolic processes. Conclusion: 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.
- Subjects
PROTEOMICS; YEAST; PRIONS; MOLECULAR chaperones; PROTEIN analysis; PROTEIN fractionation; SACCHAROMYCES cerevisiae; COMPARATIVE studies
- Publication
PLoS ONE, 2011, Vol 6, Issue 9, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0023659