Not quite the SSAme: unique roles for the yeast cytosolic Hsp70s
| Autor: | Nitika, Laura E. Knighton, Sarah K. Lotz, Gary W. Jones, Andrew W. Truman |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Gene isoform
Saccharomyces cerevisiae ved/biology.organism_classification_rank.species Biology Proteomics Article Protein Refolding Fungal Proteins 03 medical and health sciences Protein Aggregates Structure-Activity Relationship Cytosol Heat shock protein Gene Expression Regulation Fungal Yeasts Genetics Protein Isoforms HSP70 Heat-Shock Proteins Model organism 030304 developmental biology Adenosine Triphosphatases 0303 health sciences ved/biology 030302 biochemistry & molecular biology General Medicine biology.organism_classification Yeast Hsp70 Biochemistry Chaperone (protein) biology.protein Protein Processing Post-Translational Protein Binding Signal Transduction |
| Zdroj: | Curr Genet |
| Popis: | The Heat Shock Protein 70s (Hsp70s) are an essential family of proteins involved in folding of new proteins and triaging of damaged proteins for proteasomal-mediated degradation. They are highly conserved in all organisms, with each organism possessing multiple highly similar Hsp70 variants (isoforms). These isoforms have been previously thought to be identical in function differing only in their spatio-temporal expression pattern. The model organism Saccharomyces cerevisiae (baker's yeast) expresses four Hsp70 isoforms Ssa1, 2, 3 and 4. Here, we review recent findings that suggest that despite their similarity, Ssa isoforms may have unique cellular functions. |
| Databáze: | OpenAIRE |
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