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- W3080972819 abstract "Abstract Heat stress causes proteins to unfold and lose their function, jeopardizing essential cellular processes. To protect against heat and proteotoxic stress, cells mount a dedicated stress-protective programme, the so-called heat shock response (HSR). Our understanding of the mechanisms that regulate the HSR and their contributions to heat resistance and growth is incomplete. Here we employ CRISPRi/a to down- or upregulate protein kinases and transcription factors in S. cerevisiae . We measure gene functions by quantifying perturbation effects on HSR activity, thermotolerance, and cellular fitness at 23, 30 and 38°C. The integration of these phenotypes allowed us to identify core signalling pathways of heat adaptation and reveal novel functions for the high osmolarity glycerol, unfolded protein response and protein kinase A pathways in adjusting both thermotolerance and chaperone expression. We further provide evidence for unknown cross-talk of the HSR with the cell cycle-dependent kinase Cdc28, the primary regulator of cell cycle progression. Finally, we show that CRISPRi efficiency is temperature-dependent and that different phenotypes vary in their sensitivity to knock-down. In summary, our study quantifies regulatory gene functions in different aspects of heat adaptation and advances our understanding of how eukaryotic cells counteract proteotoxic and other heat-caused damage." @default.
- W3080972819 created "2020-09-01" @default.
- W3080972819 creator A5006653447 @default.
- W3080972819 creator A5008125958 @default.
- W3080972819 creator A5033185814 @default.
- W3080972819 creator A5070566112 @default.
- W3080972819 creator A5086315008 @default.
- W3080972819 date "2020-08-26" @default.
- W3080972819 modified "2023-09-23" @default.
- W3080972819 title "Gene dosage screens in yeast reveal core signalling pathways controlling heat adaptation" @default.
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