A toxic imbalance of Hsp70s inSaccharomyces cerevisiaeis caused by competition for cofactors
| Autor: | Heather L. True, Kathryn M. Keefer |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
biology Saccharomyces cerevisiae biology.organism_classification Microbiology Cofactor Yeast Hsp70 Nucleotide exchange factor 03 medical and health sciences 030104 developmental biology 0302 clinical medicine Biochemistry 030220 oncology & carcinogenesis Chaperone (protein) Toxicity biology.protein Protein folding Molecular Biology |
| Zdroj: | Molecular Microbiology. 105:860-868 |
| ISSN: | 0950-382X |
| Popis: | Summary Molecular chaperones are responsible for managing protein folding from translation through degradation. These crucial machines ensure that protein homeostasis is optimally maintained for cell health. However, ‘too much of a good thing’ can be deadly, and the excess of chaperones can be toxic under certain cellular conditions. For example, overexpression of Ssa1, a yeast Hsp70, is toxic to cells in folding-challenged states such as [PSI+]. We discovered that overexpression of the nucleotide exchange factor Sse1 can partially alleviate this toxicity. We further argue that the basis of the toxicity is related to the availability of Hsp70 cofactors, such as Hsp40 J-proteins and nucleotide exchange factors. Ultimately, our work informs future studies about functional chaperone balance and cautions against therapeutic chaperone modifications without a thorough examination of cofactor relationships. |
| Databáze: | OpenAIRE |
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