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Heat shock protein 90 kDa (Hsp90) is required for the activation and stabilization of numerous client proteins, but the functional requirements of individual clients remain poorly understood. Utilizing yeast growth assays and mutational analysis, Mishra and colleagues explore the constraints placed on Hsp90 by distinct clients and the relationship between these constraints and overall yeast fitness.
Heat shock protein 90α (Hsp90α), encoded by the HSP90AA1 gene, is the stress inducible isoform of the molecular chaperone Hsp90. Hsp90α is regulated differently and has different functions when compared to the constitutively expressed Hsp90β isoform, despite high amino acid sequence identity between the two proteins. These differences are likely due to variations in nucleotide sequence within non-coding...
The essential molecular chaperone Hsp90 functions with over ten co-chaperones in Saccharomyces cerevisiae, but the in vivo roles of many of these co-chaperones are poorly understood. Two of these co-chaperones, Cdc37 and Sgt1, target specific types of clients to Hsp90 for folding. Other co-chaperones have general roles in supporting Hsp90 function, but the degree of overlapping or competing functions...
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