Identification of novel Yap1p and Skn7p binding sites involved in the oxidative stress response of <i>Saccharomyces cerevisiae</i>

He, Xin‐Jian; Fassler, Jan S.

doi:10.1111/j.1365-2958.2005.04917.x

Cited by 80 publications

(81 citation statements)

References 33 publications

(69 reference statements)

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“…For the Dum10672 mutant, we could show that ROS accumulate around invading hyphae, while this was not observed for Dum01947 mutants. Since U. maydis lacks catalases like the YAP1-regulated CTT1 in S. cerevisiae (He and Fassler, 2005), we consider the Yap1-regulated heme peroxidase encoded by um10672 as prime activity for ROS detoxification in the U. maydis/maize system. The protein encoded by um01947 is predicted to have a mitochondrial targeting sequence; therefore, its function is likely to be confined to mitochondria.…”

Section: Discussionmentioning

confidence: 99%

AnUstilago maydisGene Involved in H2O2 Detoxification Is Required for Virulence

2007

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The fungus Ustilago maydis is a biotrophic pathogen of maize (Zea mays). In its genome we have identified an ortholog of YAP1 (for Yeast AP-1-like) from Saccharomyces cerevisae that regulates the oxidative stress response in this organism. yap1 mutants of U. maydis displayed higher sensitivity to H 2 O 2 than wild-type cells, and their virulence was significantly reduced. U. maydis yap1 could partially complement the H 2 O 2 sensitivity of a yap1 deletion mutant of S. cerevisiae, and a Yap1-green fluorescent protein fusion protein showed nuclear localization after H 2 O 2 treatment, suggesting that Yap1 in U. maydis functions as a redox sensor. Mutations in two Cys residues prevented accumulation in the nucleus, and the respective mutant strains showed the same virulence phenotype as Dyap1 mutants. Diamino benzidine staining revealed an accumulation of H 2 O 2 around yap1 mutant hyphae, which was absent in the wild type. Inhibition of the plant NADPH oxidase prevented this accumulation and restored virulence. During the infection, Yap1 showed nuclear localization after penetration up to 2 to 3 d after infection. Through array analysis, a large set of Yap1-regulated genes were identified and these included two peroxidase genes. Deletion mutants of these genes were attenuated in virulence. These results suggest that U. maydis is using its Yap1-controlled H 2 O 2 detoxification system for coping with early plant defense responses.

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Section: Discussionmentioning

confidence: 99%

AnUstilago maydisGene Involved in H2O2 Detoxification Is Required for Virulence

2007

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“…The abnormal production of ROS leads to the induction of defense mechanisms to avoid the deleterious consequence of ROS accumulation, and oxidative stress occurs when cells cannot efficiently neutralize or eliminate ROS. Several studies in the budding yeast Saccharomyces cerevisiae, including genome-wide expression profiling, have identified many genes whose transcripts or protein levels are elevated or repressed in response to oxidants (Morgan et al 1997;Godon et al 1998;Lee et al 1999;Gasch et al 2000;Cohen et al 2002;He and Fassler 2005). These studies have provided insight into the regulatory responses and the oxidative stress response regulons including the two transcription factors Yap1 and Skn7.…”

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confidence: 99%

The Rho1 GTPase Acts Together With a Vacuolar Glutathione S-Conjugate Transporter to Protect Yeast Cells From Oxidative Stress

Lee

Singh²,

Snider

et al. 2011

Genetics

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Maintenance of redox homeostasis is critical for the survival of all aerobic organisms. In the budding yeast Saccharomyces cerevisiae, as in other eukaryotes, reactive oxygen species (ROS) are generated during metabolism and upon exposure to environmental stresses. The abnormal production of ROS triggers defense mechanisms to avoid the deleterious consequence of ROS accumulation. Here, we show that the Rho1 GTPase is necessary to confer resistance to oxidants in budding yeast. Temperature-sensitive rho1 mutants (rho1 ts ) are hypersensitive to oxidants and exhibit high accumulation of ROS even at a semipermissive temperature. Rho1 associates with Ycf1, a vacuolar glutathione S-conjugate transporter, which is important for heavy metal detoxification in yeast. Rho1 and Ycf1 exhibit a two-hybrid interaction with each other and form a bimolecular fluorescent complex on the vacuolar membrane. A fluorescent-based complementation assay suggests that the GTP-bound Rho1 associates with Ycf1 and that their interaction is enhanced upon exposure to hydrogen peroxide. The rho1 ts mutants also exhibit hypersensitivity to cadmium, while cells carrying a deletion of YCF1 or mutations in a component of the Pkc1-MAP kinase pathway exhibit little or minor sensitivity to oxidants. We thus propose that Rho1 protects yeast cells from oxidative stress by regulating multiple downstream targets including Ycf1. Since both Rho1 and Ycf1 belong to highly conserved families of proteins, similar mechanisms may exist in other eukaryotes.

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“…The codependence of this large set of oxidative stress response (OXR) genes on the activity of both transcription factors has been studied in some detail (4,14,24,30,41). In contrast, only two OXR genes (DNM1 and OLA1) are reported to depend on Skn7p alone (24).…”

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confidence: 99%

Association of the Skn7 and Yap1 Transcription Factors in the Saccharomyces cerevisiae Oxidative Stress Response

Mulford

Fassler

2011

Eukaryot Cell

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Saccharomyces cerevisiae Skn7p is a stress response transcription factor that undergoes aspartyl phosphorylation by the Sln1p histidine kinase. Aspartyl phosphorylation of Skn7p is required for activation of genes required in response to wall stress, but Skn7p also activates oxidative stress response genes in an aspartyl phosphorylation-independent manner. The presence of binding sites for the Yap1p and Skn7p transcription factors in oxidative stress response promoters and the oxidative stress-sensitive phenotypes of SKN7 and YAP1 mutants suggest that these two factors work together. We present here evidence for a DNA-independent interaction between the Skn7 and Yap1 proteins that involves the receiver domain of Skn7p and the cysteinerich domains of Yap1p. The interaction with Yap1p may help partition the Skn7 protein to oxidative stress response promoters when the Yap1 protein accumulates in the nucleus.

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Identification of novel Yap1p and Skn7p binding sites involved in the oxidative stress response of Saccharomyces cerevisiae

Cited by 80 publications

References 33 publications

AnUstilago maydisGene Involved in H2O2 Detoxification Is Required for Virulence

AnUstilago maydisGene Involved in H2O2 Detoxification Is Required for Virulence

The Rho1 GTPase Acts Together With a Vacuolar Glutathione S-Conjugate Transporter to Protect Yeast Cells From Oxidative Stress

Association of the Skn7 and Yap1 Transcription Factors in the Saccharomyces cerevisiae Oxidative Stress Response

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