Proteomic Analysis of Yeast Protein Fractions Affecting Sup35p Aggregation
Author Information
Author(s): Redeker Virginie, Hughes Chris, Savistchenko Jimmy, Vissers Johannes P. C., Melki Ronald
Primary Institution: Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France
Hypothesis
What proteins modulate the aggregation of the yeast prion Sup35p?
Conclusion
The study identifies over 300 proteins that influence Sup35p aggregation and highlights the complexity of cellular changes during [PSI+] formation.
Supporting Evidence
- The study provides a comprehensive inventory of proteins involved in Sup35p aggregation.
- Proteins identified include those involved in translation, folding, and metabolic processes.
- Significant differences in protein composition were observed between [PSI+] and [psi−] yeast strains.
Takeaway
Researchers found many proteins that help or hinder the clumping of a yeast protein linked to disease, showing how complicated this process is.
Methodology
The study used a gel-free and label-free LC-MS approach to analyze yeast protein fractions.
Limitations
The study primarily focuses on yeast and may not directly translate to other organisms.
Statistical Information
P-Value
0.03
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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