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Saccharomyces cerevisiae

ABSTRACT: The yeast Snt2 protein helps coordinate the transcriptional response to hydrogen-peroxide mediated oxidative stress (RNA-seq)

PROVIDER: PRJNA184040 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR636633.fastq.gz	Fastqsanger.gz
	SRR636634.fastq.gz	Fastqsanger.gz
	SRR636635.fastq.gz	Fastqsanger.gz
	SRR636636.fastq.gz	Fastqsanger.gz
	SRR636637.fastq.gz	Fastqsanger.gz

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Saccharomyces cerevisiae

Project description:The yeast Snt2 protein helps coordinate the transcriptional response to hydrogen-peroxide mediated oxidative stress (H2O2)

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Saccharomyces cerevisiae

Project description:The yeast Snt2 protein helps coordinate the transcriptional response to hydrogen-peroxide mediated oxidative stress (rapamycin or DMSO)

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Project description:The yeast Snt2 protein helps coordinate the transcriptional response to hydrogen-peroxide mediated oxidative stress

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Transcription profiling of Saccharomyces cerevisiae reveals the Cbf1 basic helix-loop-helix transcription factor is required for the response to hydrogen peroxide stress

Project description:Cbf1 is a basic helix-loop-helix transcription factor which regulates the expression of many genes of the sulphur assimilation pathway in yeast. Gamma-glutamylcysteine synthetase (GSH1), encoding the rate-limiting enzyme in glutathione biosynthesis, is constitutively elevated in cbf1 mutants indicating that Cbf1 normally represses GSH1 expression. We used transcriptional profiling to show that a number of antioxidant and stress genes are similarly repressed by Cbf1, consistent with the high oxidant tolerance of cbf1 mutants. Our data indicate that Cbf1 plays a key role in the regulation of gene expression during oxidative stress conditions induced by exposure to hydrogen peroxide. The Yap1 transcription factor induces GSH1 expression in response to hydrogen peroxide in a mechanism that does not require the Met4 transcription factor to overcome the inhibitory action of Cbf1. We show that hydrogen peroxide does not affect Cbf1 occupancy on the GSH1 promoter, but results in specific modification of Cbf1 by phosphorylation. Our data indicate that casein kinase (CK2) can directly phosphorylate Cbf1 in vitro. Furthermore, CK2 activity is required to phosphorylate Cbf1 and induce GSH1 expression in yeast cells in response to hydrogen peroxide. CK2 mutants are sensitive to hydrogen peroxide consistent with a role for CK2 in regulating the cellular response to oxidative stress. CK2 is a ubiquitous serine/threonine protein kinase and the finding that it is regulated by oxidative stress is particularly interesting, since there is increasing evidence that it is involved in a number of pathological conditions including cancer, neurodegenerative and cardiovascular diseases.

2009-10-01 | E-MEXP-2159 | biostudies-arrayexpress

Saccharomyces cerevisiae

Project description:Time course of oxidative stress responses in yeast, caused by Menadione or hydrogen peroxide

| PRJNA91503 | ENA

Saccharomyces cerevisiae

Project description:Adaptation to hydrogen peroxide

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Saccharomyces cerevisiae mRBPome in oxidative stress conditions

Project description:This project aims to identify novel RNA binding proteins in the baker's yeast , Saccharomyces cerevisiae, involved in the oxidative stress,. Since interactions between RNAs and proteins may be transient, yeast cells, either untreated and growth in rich media and exposed to 0.5 mM hydrogen peroxide for 15 minutes were crosslinked with UV light at 254 nm which promotes the covalent link between proteins and RNAs. After this, polyadenylated mRNAs were purified via oligo(dT) coupled to magentic beads under stringent conditions. Finally, samples were subjected to mass spectrometry analysis. To rule out the possibility of RNA-independent binding we also analysed other samples where we performed competition assays with polyadenylic acid

2021-06-10 | PXD005943 | Pride

Saccharomyces cerevisiae

Project description:Expression data from yeast wild type (WT) and sod1Δ strains after treatment with hydrogen peroxide (H2O2)

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Response of Saccharomyces cerevisiae (Dal80Δ) to linoleic acid hydroperoxide

Project description:Oxidative stress is experienced by all aerobic organisms and results in cellular damage. The damage caused during oxidative stress is particular to the oxidant challenge faced, and so too is the induced stress response. The eukaryote Saccharomyces cerevisiae is sensitive to low concentrations of the lipid hydroperoxide - linoleic acid hydroperoxide (LoaOOH) - and its response is unique relative to other peroxide treatments. Part of the yeast response to LoaOOH includes a change in the cellular requirement for nutrients, such as sulfur, nitrogen and various metal ions. The metabolism of sulfur is involved in antioxidant defence, although the role nitrogen during oxidative stress is not well understood. Investigating the response induced by yeast to overcome LoaOOH exposure, with a particular focus on nitrogen metabolism, will lead to greater understanding of how eukaryotes survive lipid hydroperoxide-induced stress, and associated lipid peroxidation, which occurs in the presence of polyunsaturated fatty acids. We used genome-wide microarrays to investigate the changes in gene expression of S. cerevisiae (Dal80Δ) to LoaOOH-induced oxidative stress.

2014-02-13 | GSE54951 | GEO

Transcription profiling of S. cerevisiae mRNA abundance following oxidative stress and DNA damage stress

Project description:We subjected yeast to two stresses, oxidative stress, which under current settings induces a fast and transient response in mRNA abundance, and DNA damage, which triggers a slow enduring response. Using microarrays we performed a conventional quantification of change in mRNA abundance. Experiment Overall Design: We used Affymetrix microarrays to quantify changes in mRNA abundance following oxidative stress (using hydrogen peroxide) and DNA damage stress (using methyl methanesulfonate) during a three-hour time course (0, 30 min, 60 min, 100 min, 140 min, 180 min).

2008-10-26 | E-GEOD-12220 | biostudies-arrayexpress

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