Expression of a Glutamate Decarboxylase Homologue Is Required for Normal Oxidative Stress Tolerance in Saccharomyces cerevisiae

Coleman, Sean T.; Fang, Tung K.; Rovinsky, Sherry A.; Turano, Frank J.; Moye‐Rowley, W. Scott

doi:10.1074/jbc.m007103200

Cited by 197 publications

(162 citation statements)

References 47 publications

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“…Two proteins are putative stress proteins, like the heat shock protein AN10202 (homologous to Ssa1p in yeast), or the GABA transaminase (AN2248), which homologous protein in yeast is involved in oxidative stress response (Coleman et al, 2001). We identified histone-2B as the only histone which could be an interaction partner of SasA.…”

Section: Protein Interaction Studies Revealed Involvement Of Sasa In mentioning

confidence: 99%

Fungal S-adenosylmethionine synthetase and the control of development and secondary metabolism in Aspergillus nidulans

Gerke

Bayram

Braus

2012

Fungal Genetics and Biology

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a b s t r a c tThe filamentous fungus Aspergillus nidulans carries a single gene for the S-adenosylmethionine (SAM) synthetase SasA, whereas many other organisms possess multiple SAM synthetases. The conserved enzyme catalyzes the reaction of methionine and ATP to the ubiquitous methyl group donor SAM. SAM is the main methyl group donor for methyltransferases to modify DNA, RNA, protein, metabolites, or phospholipid target substrates. We show here that the single A. nidulans SAM synthetase encoding gene sasA is essential. Overexpression of sasA, encoding a predominantly cytoplasmic protein, led to impaired development including only small sterile fruiting bodies which are surrounded by unusually pigmented auxiliary Hülle cells. Hülle cells are the only fungal cell type which does not contain significant amounts of SasA. Sterigmatocystin production is altered when sasA is overexpressed, suggesting defects in coordination of development and secondary metabolism. SasA interacts with various metabolic proteins including methionine or mitochondrial metabolic enzymes as well as proteins involved in fungal morphogenesis. SasA interaction to histone-2B might reflect a putative epigenetic link to gene expression. Our data suggest a distinct role of SasA in coordinating fungal secondary metabolism and development.

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Section: Protein Interaction Studies Revealed Involvement Of Sasa In mentioning

confidence: 99%

Fungal S-adenosylmethionine synthetase and the control of development and secondary metabolism in Aspergillus nidulans

Gerke

Bayram

Braus

2012

Fungal Genetics and Biology

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“…Previous studies have demonstrated that S. cerevisiae mutants lacking UGA1, UGA2 and UGA3 are incapable of growth on minimal medium with GABA as the sole nitrogen source, but grow normally on minimal medium with ammonium sulphate as the sole nitrogen source (Ramos et al, 1985;Coleman et al, 2001). To test the extent of interchangeable function of AtGABA-T and ScGABA-TKG in the cytosol and mitochondria, Δuga1 mutant was transformed with plasmid constructs containing AtGABA-T, with and without the mitochondrial targeting peptide or containing ScGABA-TKG or ScGABA-TKG with the mitochondrial targeting peptide.…”

Section: Gaba Transaminasesmentioning

confidence: 99%

GABA transaminases from Saccharomyces cerevisiae and Arabidopsis thaliana complement function in cytosol and mitochondria

Cao

Barbosa

Singh

et al. 2013

Yeast

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GABA transaminase (GABA-T) catalyses the conversion of GABA to succinate semialdehyde (SSA) in the GABA shunt pathway. The GABA-T from Saccharomyces cerevisiae (ScGABA-TKG) is an α-ketoglutarate-dependent enzyme encoded by the UGA1 gene, while higher plant GABA-T is a pyruvate/glyoxylate-dependent enzyme encoded by POP2 in Arabidopsis thaliana (AtGABA-T). The GABA-T from A. thaliana is localized in mitochondria and mediated by an 18-amino acid N-terminal mitochondrial targeting peptide predicated by both web-based utilities TargetP 1.1 and PSORT. Yeast UGA1 appears to lack a mitochondrial targeting peptide and is localized in the cytosol. To verify this bioinformatic analysis and examine the significance of ScGABA-TKG and AtGABA-T compartmentation and substrate specificity on physiological function, expression vectors were constructed to modify both ScGABA-TKG and AtGABA-T, so that they express in yeast mitochondria and cytosol. Physiological function was evaluated by complementing yeast ScGABA-TKG deletion mutant Δuga1 with AtGABA-T or ScGABA-TKG targeted to the cytosol or mitochondria for the phenotypes of GABA growth defect, thermosensitivity and heat-induced production of reactive oxygen species (ROS). This study demonstrates that AtGABA-T is functionally interchangeable with ScGABA-TKG for GABA growth, thermotolerance and limiting production of ROS, regardless of location in mitochondria or cytosol of yeast cells, but AtGABA-T is about half as efficient in doing so as ScGABA-TKG. These results are consistent with the hypothesis that pyruvate/glyoxylate-limited production of NADPH mediates the effect of the GABA shunt in moderating heat stress in Saccharomyces.

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“…NADPH can also be synthesized via succinate semialdehyde dehydrogenase encoded by the CESR gene SPAC139.05. A role for this enzyme in the response to stress has been suggested in S. cerevisiae (Coleman et al, 2001). Other CESR genes encode antioxidants such as catalase (cta1), glutathione peroxidase (gpx1), thioredoxin (trx2), glutaredoxin (grx1), glutathione-Stransferase (SPAC688.04), and metallothioneine (zym1), predicted protease genes (SPCC4G3.03, SPCC338.12, and isp6) as well as a gene involved in ubiquitination (SPAC2C4.15c) and gpd1 (encoding glycerol-3-phosphate dehydrogenase).…”

Section: Global Stress Responses In Fission Yeastmentioning

confidence: 99%

Global Transcriptional Responses of Fission Yeast to Environmental Stress

Chen

Toone

Mata

et al. 2003

MBoC

727

971

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We explored transcriptional responses of the fission yeast Schizosaccharomyces pombe to various environmental stresses. DNA microarrays were used to characterize changes in expression profiles of all known and predicted genes in response to five stress conditions: oxidative stress caused by hydrogen peroxide, heavy metal stress caused by cadmium, heat shock caused by temperature increase to 39°C, osmotic stress caused by sorbitol, and DNA damage caused by the alkylating agent methylmethane sulfonate. We define a core environmental stress response (CESR) common to all, or most, stresses. There was a substantial overlap between CESR genes of fission yeast and the genes of budding yeast that are stereotypically regulated during stress. CESR genes were controlled primarily by the stress-activated mitogen-activated protein kinase Sty1p and the transcription factor Atf1p. S. pombe also activated gene expression programs more specialized for a given stress or a subset of stresses. In general, these "stress-specific" responses were less dependent on the Sty1p mitogen-activated protein kinase pathway and may involve specific regulatory factors. Promoter motifs associated with some of the groups of coregulated genes were identified. We compare and contrast global regulation of stress genes in fission and budding yeasts and discuss evolutionary implications.

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Expression of a Glutamate Decarboxylase Homologue Is Required for Normal Oxidative Stress Tolerance in Saccharomyces cerevisiae

Cited by 197 publications

References 47 publications

Fungal S-adenosylmethionine synthetase and the control of development and secondary metabolism in Aspergillus nidulans

Fungal S-adenosylmethionine synthetase and the control of development and secondary metabolism in Aspergillus nidulans

GABA transaminases from Saccharomyces cerevisiae and Arabidopsis thaliana complement function in cytosol and mitochondria

Global Transcriptional Responses of Fission Yeast to Environmental Stress

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