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Transcription profiling by array of Saccharomyces cerevisiae with genotypes: wild type, wild type with constitutive hsf1 activation, hac1∆ and hac1∆ with constitutive hsf1 activation


ABSTRACT: In the yeast Saccharomyces cerevisiae, accumulation of misfolded proteins in the endoplasmic reticulum (ER) causes ER stress and activates the unfolded protein response (UPR) mediated by Hac1p, whereas the heat shock response (HSR) mediated by Hsf1p mainly regulates cytosolic processes and protects the cell from different stresses. In this study, we find that a constitutive activation of the HSR by over-expression of a mutant HSF1 gene could relieve ER stress in both wild type and hac1∆ UPR-deficient cells. We studied the genome-wide transcriptional response in order to identify regulatory mechanisms that govern the interplay between UPR and HSR responses. Interestingly, we find that the regulation of ER stress via HSR is mainly through facilitation of protein folding and secretion and not via the induction of Rpn4-dependent proteasomal activity. Four Saccharomyces cerevisiae strains, WT, WT(hsf1), hac1∆ and hac1∆(hsf1), were grown in SD-URA medium and treated with 2.5 mM DTT. After two hours induction, samples were taken for RNA extraction and hybridization on Affymetrix microarrays. Biological triplicates were applied.

OTHER RELATED OMICS DATASETS IN: PRJNA170538

PROVIDER: E-GEOD-39311 | ExpressionAtlas | 2014-07-10

REPOSITORIES: ExpressionAtlas

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Publications

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

Hou Jin J   Tang Hongting H   Liu Zihe Z   Österlund Tobias T   Nielsen Jens J   Petranovic Dina D  

FEMS yeast research 20131212 3


In yeast Saccharomyces cerevisiae, accumulation of misfolded proteins in the endoplasmic reticulum (ER) causes ER stress and activates the unfolded protein response (UPR), which is mediated by Hac1p. The heat shock response (HSR) mediated by Hsf1p, mainly regulates cytosolic processes and protects the cell from stresses. Here, we find that a constitutive activation of the HSR could increase ER stress resistance in both wild-type and UPR-deficient cells. Activation of HSR decreased UPR activation  ...[more]

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