Genome-wide expression analyses of adaptive response against medadione-induced oxidative stress in Saccharomyces cerevisiae KNU5377

2006 ◽  
Vol 41 (11) ◽  
pp. 2305-2313 ◽  
Author(s):  
Ilsup Kim ◽  
Haesun Yun ◽  
Hitoshi Iwahashi ◽  
Ingnyol Jin
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Adaptive Response ◽  
Genome Wide ◽  
Genome Wide Expression ◽  
Saccharomyces Cerevisiae Knu5377

Genome-wide expression profile of the mnn2Δ mutant of Saccharomyces cerevisiae

2006 ◽  
Vol 89 (3-4) ◽  
pp. 485-494 ◽  
Author(s):  
Isaac Corbacho ◽  
Isabel Olivero ◽  
Stefan Hohmann ◽  
Per Sunnerhagen ◽  
Luis M. Hernández
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Expression Profile ◽  
Genome Wide ◽  
Genome Wide Expression

scholarly journals High Resistance to Oxidative Stress in the Fungal Pathogen Candida glabrata Is Mediated by a Single Catalase, Cta1p, and Is Controlled by the Transcription Factors Yap1p, Skn7p, Msn2p, and Msn4p

2008 ◽  
Vol 7 (5) ◽  
pp. 814-825 ◽  
Author(s):  
Mayra Cuéllar-Cruz ◽  
Marcela Briones-Martin-del-Campo ◽  
Israel Cañas-Villamar ◽  
Javier Montalvo-Arredondo ◽  
Lina Riego-Ruiz ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Candida Albicans ◽  
Transcription Factors ◽  
Adaptive Response ◽  
Fungal Pathogen ◽  
Candida Glabrata ◽  
Systemic Infection ◽  
Oxidative Stress Response

ABSTRACT We characterized the oxidative stress response of Candida glabrata to better understand the virulence of this fungal pathogen. C. glabrata could withstand higher concentrations of H2O2 than Saccharomyces cerevisiae and even Candida albicans. Stationary-phase cells were extremely resistant to oxidative stress, and this resistance was dependent on the concerted roles of stress-related transcription factors Yap1p, Skn7p, and Msn4p. We showed that growing cells of C. glabrata were able to adapt to high levels of H2O2 and that this adaptive response was dependent on Yap1p and Skn7p and partially on the general stress transcription factors Msn2p and Msn4p. C. glabrata has a single catalase gene, CTA1, which was absolutely required for resistance to H2O2 in vitro. However, in a mouse model of systemic infection, a strain lacking CTA1 showed no effect on virulence.

Adaptive response of Saccharomyces cerevisiae to hyperosmotic and oxidative stress

2005 ◽  
Vol 40 (11) ◽  
pp. 3614-3618 ◽  
Author(s):  
Fuping Lu ◽  
Yu Wang ◽  
Dongqing Bai ◽  
Lianxiang Du
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Adaptive Response ◽  
And Oxidative Stress

scholarly journals Importance of glucose-6-phosphate dehydrogenase in the adaptive response to hydrogen peroxide in Saccharomyces cerevisiae

1998 ◽  
Vol 330 (2) ◽  
pp. 811-817 ◽  
Author(s):  
Shingo IZAWA ◽  
Keiko MAEDA ◽  
Takeo MIKI ◽  
Junichi MANO ◽  
Yoshiharu INOUE ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Adaptive Response ◽  
Yeast Cells ◽  
Wild Type ◽  
Total Glutathione ◽  
Dependent Activity ◽  
Increased Sensitivity ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Increased Susceptibility

Glucose-6-phosphate dehydrogenase (G6PDH)-deficient cells of Saccharomyces cerevisiae showed increased susceptibility and were unable to induce adaptation to oxidative stress. Historically, mainly in human erythrocytes, it has been suggested and accepted that decreased cellular GSH, due to loss of the NADPH-dependent activity of glutathione reductase (GR), is responsible for the increased sensitivity to oxidative stress in G6PDH-deficient cells. In the present study we investigated whether the increased susceptibility and the inability to induce adaptation to H2O2 stress of G6PDH-deficient yeast is caused by incompleteness of glutathione recycling. We constructed G6PDH- and GR-deficient mutants and analysed their adaptive response to H2O2 stress. Although G6PDH-deficient cells contained comparable amounts of GSH and GR activity to wild-type cells, GSSG was not reduced efficiently, and intracellular GSSG levels and the ratio of GSSG to total glutathione (GSSG/tGSH) were higher in G6PDH-deficient cells than in wild-type. On the other hand, GR-deficient cells showed a susceptibility identical with that of wild-type cells and induced adaptation to H2O2 stress, even though the GSSG/tGSH ratio in GR-deficient cells was higher than in G6PDH-deficient cells. These results indicate that incompleteness of glutathione recycling alone is not sufficient to account for the increased sensitivity and inability to induce adaptation to H2O2 stress of G6PDH-deficient yeast cells. In S. cerevisiae, G6PDH appears to play other important roles in the adaptive response to H2O2 stress besides supplying NADPH to the GR reaction.

scholarly journals The Genome-Wide Early Temporal Response of Saccharomyces cerevisiae to Oxidative Stress Induced by Cumene Hydroperoxide

PLoS ONE ◽  
2013 ◽  
Vol 8 (9) ◽  
pp. e74939 ◽  
Author(s):  
Wei Sha ◽  
Ana M. Martins ◽  
Reinhard Laubenbacher ◽  
Pedro Mendes ◽  
Vladimir Shulaev
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Cumene Hydroperoxide ◽  
Temporal Response ◽  
Genome Wide

Modulation of the specific glutathionylation of mitochondrial proteins in the yeast Saccharomyces cerevisiae under basal and stress conditions

2017 ◽  
Vol 474 (7) ◽  
pp. 1175-1193 ◽  
Author(s):  
Rachel Gergondey ◽  
Camille Garcia ◽  
Christophe H. Marchand ◽  
Stephane D. Lemaire ◽  
Jean-Michel Camadro ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Adaptive Response ◽  
Metabolic Response ◽  
Covalent Binding ◽  
Redox Status ◽  
Stress Conditions ◽  
Post Translational Modification ◽  
Yeast Saccharomyces Cerevisiae ◽  
Protein Thiols

The potential biological consequences of oxidative stress and changes in glutathione levels include the oxidation of susceptible protein thiols and reversible covalent binding of glutathione to the –SH groups of proteins by S-glutathionylation. Mitochondria are central to the response to oxidative stress and redox signaling. It is therefore crucial to explore the adaptive response to changes in thiol-dependent redox status in these organelles. We optimized the purification protocol of glutathionylated proteins in the yeast Saccharomyces cerevisiae and present a detailed proteomic analysis of the targets of protein glutathionylation in cells undergoing constitutive metabolism and after exposure to various stress conditions. This work establishes the physiological importance of the glutathionylation process in S. cerevisiae under basal conditions and provides evidence for an atypical and unexpected cellular distribution of the process between the cytosol and mitochondria. In addition, our data indicate that each oxidative condition (diamide, GSSG, H2O2, or the presence of iron) elicits an adaptive metabolic response affecting specific mitochondrial metabolic pathways, mainly involved in the energetic maintenance of the cells. The correlation of protein modifications with intracellular glutathione levels suggests that protein deglutathionylation may play a role in protecting mitochondria from oxidative stress. This work provides further insights into the diversity of proteins undergoing glutathionylation and the role of this post-translational modification as a regulatory process in the adaptive response of the cell.

scholarly journals Genome-wide map of Apn1 binding sites under oxidative stress in Saccharomyces cerevisiae

Yeast ◽  
2017 ◽  
Vol 34 (11) ◽  
pp. 447-458 ◽  
Author(s):  
Lydia P. Morris ◽  
Andrew B. Conley ◽  
Natalya Degtyareva ◽  
I. King Jordan ◽  
Paul W. Doetsch
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Binding Sites ◽  
Genome Wide

scholarly journals Yap1 Accumulates in the Nucleus in Response to Carbon Stress in Saccharomyces cerevisiae

2003 ◽  
Vol 2 (1) ◽  
pp. 19-26 ◽  
Author(s):  
Heather A. Wiatrowski ◽  
Marian Carlson
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Adaptive Response ◽  
Fluorescent Protein ◽  
Nuclear Accumulation ◽  
Glucose Limitation ◽  
Ionic Stress ◽  
Green Fluorescent ◽  
Two Hybrid ◽  
Carbon Stress

ABSTRACT Yap1 is a transcription factor of the AP-1 family that is required for the adaptive response to oxidative stress in Saccharomyces cerevisiae. We recovered Yap1 in a two-hybrid screen for proteins that interact with the Sip2 subunit of the Snf1 protein kinase, which is required for the adaptation of cells to glucose limitation. Yap1 becomes enriched in the nucleus when cells are subjected to oxidative stress. We show that the localization of Yap1 is similarly sensitive to carbon stress. When glucose-grown cells were shifted to medium containing glycerol or no added carbon source, green fluorescent protein (GFP)-Yap1 accumulated in the nucleus. After adaptation to growth in glycerol, GFP-Yap1 was again primarily cytoplasmic. Nuclear accumulation was independent of respiration and of the Snf1, PKA, TOR, and Yak1 pathways, and the mechanism is distinct from that involved in the response to hydrogen peroxide. Addition of glutathione to the medium inhibited nuclear accumulation of GFP-Yap1 in response to carbon stress but did not affect the relocalization of Gal83 or Mig1. Other stresses such as increased temperature, acidic pH, and ionic stress did not cause nuclear enrichment of GFP-Yap1. These findings suggest a role for Yap1 in the response to carbon stress.

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