The heat shock response relies on orthogonal mechanisms to maintain protein homeostasis in yeast

We globally analyzed the heat stress response (HSR) in yeast on the transcriptomic, tranlatomic and the proteomic level. The cells were stressed at 37 °C, 42 °C and 46 °C and the fractionated proteomes measured on a Fusion mass spectrometer. With this approach we were able to reveal a modular character of the HSR dependent on the severity of the stress. We showed that at temperatures up to 42 °C besides upregulation of stress protective factors refilling the pool of degraded and aggregating proteins is an important branch of the HSR. Whereas, at sublethal temperatures (46 °C) lots of aggregation and phase transition processes were observed. This is part two of the pride submission and only contains the proteomic data under inhibition of the proteasome with bortezomib.