Management of the endoplasmic reticulum stress by activation of the heat shock response in yeast.

摘要: In yeast Saccharomyces cerevisiae, accumulation of misfolded proteins in the endoplasmic reticulum (ER) causes ER stress and activates unfolded protein response (UPR), which is mediated by Hac1p. The heat shock (HSR) Hsf1p, mainly regulates cytosolic processes protects cell from stresses. Here, we find that a constitutive activation HSR could increase resistance both wild-type UPR-deficient cells. Activation decreased UPR WT (as shown HAC1 mRNA splicing). We analyzed genome-wide transcriptional order to propose regulatory mechanisms govern interplay between followed up for hypotheses experiments vivo vitro. Interestingly, found regulation via (1) only partially dependent on over-expression Kar2p (ER resident chaperone induced stress); (2) does not involve turnover proteasome activity; (3) related oxidative response. From transcription data, also enhances through facilitation folding secretion. coordinates multiple stress-response pathways, including repression overall translation.