The heat shock response in yeast is modular and maintains protein homeostasis via distinct mechanisms

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 and Q-Exactive Plus (both Thermo) mass spectrometer, respectively. 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.