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Chaperoning the Proteome

Molecular chaperones are critical to maintaining cellular protein homeostasis. There are several families of chaperones in the cell with some being specific for certain substrates, while others act on many protein targets. As a result, chaperones are expected to be involved in many cellular pathways with only a few being well elucidated. To obtain a comprehensive view of chaperone function in the cell, we developed an integrative approach based on systematic physical and genetic interaction mapping to decipher interactions involving all main chaperones (67) and cochaperones (15) of Saccharomyces cerevisiae. The analysis revealed novel chaperone substrates and novel chaperone activities. As part of this analysis, we unexpectedly found that many interactors of the Hsp90 chaperone system are proteins that form foci under stress conditions. Such foci forming tendency was then demonstrated for the highly conserved AAA+ ATPases Rvb1 and Rvb2 that are part of the R2TP complex that interacts with Hsp90. In response to nutrient deprivation, a fraction of Rvb1 and Rvb2 colocalize to perinuclear foci that dissolve upon nutrient addition. We propose that foci formation might be a feature of many chaperone substrates.