The effect of stress on biophysical characteristics of misfolded protein aggregates in living Saccharomyces cerevisiae cells.
Exp Gerontol
; 162: 111755, 2022 06 01.
Article
en En
| MEDLINE
| ID: mdl-35240259
ABSTRACT
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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas de Saccharomyces cerevisiae
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Exp Gerontol
Año:
2022
Tipo del documento:
Article
País de afiliación:
Suecia