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Saccharomyces cerevisiae

ABSTRACT: IRE1-dependent gene induction upon tunicamycin stress in S. cerevisiae cells

PROVIDER: PRJDB18395 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	DRR576930_1.fastq.gz	Fastqsanger.gz
	DRR576930_2.fastq.gz	Fastqsanger.gz
	DRR576931_1.fastq.gz	Fastqsanger.gz
	DRR576931_2.fastq.gz	Fastqsanger.gz
	DRR576932_1.fastq.gz	Fastqsanger.gz

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Saccharomyces cerevisiae

Project description:IRE1-dependent gene induction in Saccharomyces cerevisiae

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IRE1-dependent transcriptional change under a canonical endoplasmic-reticulum stressing stimulus and upon diauxic shift in Saccharomyces cerevisiae cells

Project description:Ire1 is an endoplasmic reticulum (ER)-located transmembrane protein that triggers the unfolded protein response. I recently noticed that Ire1 is activated not only in response to ER accumulation of unfolded proteins but also alongside diauxic shift in yeast Saccharomyces cerevisiae cells. I thus asked how different the Ire1-target genes upon two distinct scenes, a canonical ER -stressing stimuli and diauxic shift. Thus NGS transcriptome analysis was performed by using IRE1+ and ire1-delta mutant yeast cells under these conditions.

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Sse1, Hsp110 chaperone of yeast, controls the cellular fate during Endoplasmic Reticulum-stress

Project description:Sse1, yeast cytosolic Hsp110 chaperone, is a wellknown Nucleotide Exchange Factor (NEF), a protein-disaggregase and a Chaperone linked to Protein Synthesis (CLIPS). Here we demonstrate SSE1’s genetic interaction with IRE1 and HAC1, the Endoplasmic Reticulum-Unfolded Protein Response (ER-UPR) sensors. sse1Δ strain exhibits an ER-UPR signalling-dependent resistance to tunicamycin-induced ER stress. Importantly, ER-stress-responsive reorganization of translating ribosomes from polysomes to monosomes is inefficient in SSE1 deleted strain leading to uninterrupted protein translation and starkly different ER-UPR kinetics. sse1Δ exhibits faster ER-UPR induction and quicker reversal to basal state compared to wildtype (WT) cells. Interestingly, ER-stress mediated yeast cell division arrest is escaped in sse1Δ strain during long term tunicamycin stress indicating important role of this chaperone in controlling cell division during ER stress. Furthermore, sse1Δ strain shows significantly higher cell viability in comparison to WT yeast, following short-term as well as long-term tunicamycin stress. In summary, we show that cytosolic chaperone Sse1 genetically interacts with ER-UPR pathway, controls the kinetics of ER-UPR, stress-induced cell division arrest and cell viability during global ER stress by tunicamycin.

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Expression data from Saccharomyces cerevisiae WT, WT(hsf1), hac1∆ and hac1∆(hsf1)

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