Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones
| Autor: | Jason E. Gestwicki, Anne T. Gillies, Rebecca Taylor |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Biochemistry & Molecular Biology
Saccharomyces cerevisiae Proteins GTPase-activating protein 1.1 Normal biological development and functioning Saccharomyces cerevisiae Vesicular Transport Proteins Ribosome biogenesis Article Underpinning research HSP70 Heat-Shock Proteins Molecular Biology biology HSP40 Heat-Shock Proteins biology.organism_classification Phosphoproteins Calmodulin-binding proteins Hsp70 Cell biology Calmodulin-Binding Proteins Patient Safety Generic health relevance Biochemistry and Cell Biology Signal transduction Protein quality Biotechnology Molecular Chaperones Signal Transduction |
| Zdroj: | Molecular bioSystems, vol 8, iss 11 |
| ISSN: | 1742-2051 |
| Popis: | J proteins are a diverse family of co-chaperones that cooperate with heat shock protein 70 (Hsp70) to coordinate protein quality control, especially in response to cellular stress. Current models suggest that individual J proteins might play roles in recruiting Hsp70s to specific functions, such as maintaining cell wall integrity or promoting ribosome biogenesis. However, relatively few stresses have been used to test this model and, as a result, only a few specific activities have been identified. To expand our understanding of the J protein network, we used a synthetic lethal approach in which 11 Saccharomyces cerevisiae deletion strains were treated with 12 well-characterized chemical inhibitors. The results defined new roles for specific J proteins in major signaling pathways. For example, an important role for Swa2 in cell wall integrity was identified and activities of the under-explored Jjj1, Apj1, Jjj3 and Caj1 proteins were suggested. More generally, these findings support a model in which some J proteins, such as Ydj1 and Zuo1, play “generalist” roles, while others, such as Apj1 and Jjj2, are “specialists”, having roles in relatively few pathways. Together, these results provide new insight into the network of J proteins. |
| Databáze: | OpenAIRE |
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