The effect of stress on biophysical characteristics of misfolded protein aggregates in living Saccharomyces cerevisiae cells
Review article, 2022

Aggregation of misfolded or damaged proteins is often attributed to numerous metabolic and neurodegenerative disorders. To reveal underlying mechanisms and cellular responses, it is crucial to investigate protein aggregate dynamics in cells. Here, we used super-resolution single-molecule microscopy to obtain biophysical characteristics of individual aggregates of a model misfolded protein ∆ssCPY* labelled with GFP. We demonstrated that oxidative and hyperosmotic stress lead to increased aggregate stoichiometries but not necessarily the total number of aggregates. Moreover, our data suggest the importance of the thioredoxin peroxidase Tsa1 for the controlled sequestering and clearance of aggregates upon both conditions. Our work provides novel insights into the understanding of the cellular response to stress via revealing the dynamical properties of stress-induced protein aggregates.

Super-resolution single-molecule microscopy


Stress-induced protein aggregation


Protein quality control


Barbara Maria Schnitzer

Chalmers, Mathematical Sciences, Applied Mathematics and Statistics

University of Gothenburg

Niek Welkenhuysen

Chalmers, Biology and Biological Engineering, Systems and Synthetic Biology

University of Gothenburg

Mark C. Leake

University of York

Sviatlana Shashkova

University of Gothenburg

University of York

Marija Cvijovic

University of Gothenburg

Chalmers, Mathematical Sciences, Applied Mathematics and Statistics

Experimental Gerontology

0531-5565 (ISSN)

Vol. 162 111755

Subject Categories

Biochemistry and Molecular Biology


Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)



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6/3/2022 8