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Updated: Jun 5, 2026
11:04
Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
Published on: June 23, 2018
Linking amyloid protein aggregation and yeast survival.
Montse Morell1, Natalia S de Groot, Josep Vendrell
1Departament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, E-08193 Bellaterra, Spain. salvador.ventura@uab.es
Molecular Biosystems
|January 18, 2011
Summary
A novel yeast-based assay monitors protein aggregation in vivo by linking target protein solubility to cell survival. This method screens compounds and genes affecting amyloid diseases like Alzheimer's.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Protein aggregation and amyloid formation are implicated in numerous human diseases.
- Assessing intracellular protein solubility in vivo is crucial for understanding disease mechanisms.
Purpose of the Study:
- To develop a general method for assessing intracellular solubility of amyloid proteins in eukaryotic cells.
- To enable in vivo screening of genes and compounds that modulate protein aggregation.
Main Methods:
- A fusion protein approach linking target protein aggregation to dihydrofolate reductase (DHFR) activity.
- Utilizing yeast cell survival in the presence of methotrexate as a readout for protein solubility.
- In vivo visualization of protein aggregation and cellular localization.
Main Results:
- Demonstrated the assay's applicability using models like Alzheimer's amyloid beta, huntingtin polyglutamine expansions, and alpha-synuclein.
- Successfully evaluated the anti-aggregational effects of small molecules.
- Assessed the impact of yeast protein quality control machinery on aggregation.
Conclusions:
- The aggregation reporter system provides a versatile tool for studying amyloid protein aggregation in vivo.
- This method facilitates high-throughput screening for therapeutic interventions against protein aggregation diseases.
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