Hydrogen peroxide-induced carbonylation of key metabolic enzymes in Saccharomyces cerevisiae: the involvement of the oxidative stress response regulators Yap1 and Skn7

Costa, Vítor Santos; Amorim, Maria Amélia; Quintanilha, Alexandre; Moradas‐Ferreira, Pedro

doi:10.1016/s0891-5849(02)01086-9

Cited by 135 publications

(105 citation statements)

References 47 publications

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“…Sod1p has been reported to be carbonylated in wild-type yeast strains grown on glucose following a challenge with hydrogen peroxide [24]. We also observed carbonylation of Sod1p in the Δidp2Δzwf1 mutant shifted to oleate medium.…”

Section: Discussionsupporting

confidence: 61%

“…In particular, all of the glycolytic and cytosolic metabolic enzymes listed in Table 3, with the exception of Lys9p, were identified in both types of studies [24,46,47]. In other functional categories, Sod1p and cyclophilin Cpr1p were similarly identified as carbonylated in the Δidp2Δzwf1 mutant shifted to oleate medium, and in wild-type glucose-grown hydrogen peroxide-challenged cells [24]. Other carbonylated proteins, including Tsa1p, Ahp1p, Hsp26p, Adh3p, and Mcr1p, were uniquely identified in the Δidp2Δzwf1 mutant.…”

Section: Discussionmentioning

confidence: 95%

“…(b) Many of these fluorescein-labeled proteins exhibit multiple isoforms (labeled with letters) with slight differences in apparent molecular weights and isoelectric points. Multiple isoforms are common in two-dimensional analyses of yeast cellular proteins [24][25][26][27][28]. (c) Many of the same proteins were found to contain disulfide bonds in oleate-shifted cells (gels not shown).…”

Section: Assays For Disulfide Bondsmentioning

confidence: 99%

“…(These effects were much less pronounced with a shift of the mutant strain to acetate medium.) We used two-dimensional electrophoresis to examine carbonylated proteins in the mutant strain shifted to oleate in the absence or presence of glutathione and DTT, with the goal of comparing results with our data on disulfide bond-containing proteins, as well as with results of several reported studies of carbonylation in yeast cells grown on glucose with exogenous oxidants [24,46,47].…”

Section: Specific Proteins Modified By Carbonylationmentioning

confidence: 99%

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Changes in disulfide bond content of proteins in a yeast strain lacking major sources of NADPH

Minard

Carroll

Weintraub

et al. 2007

Free Radical Biology and Medicine

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A yeast mutant lacking the two major cytosolic sources of NADPH, glucose-6-phosphate dehydrogenase (Zwf1p) and NADP + -specific isocitrate dehydrogenase (Idp2p), has been demonstrated to lose viability when shifted to medium with acetate or oleate as the carbon source. This loss in viability was found to correlate with an accumulation of endogenous oxidative byproducts of respiration and peroxisomal β-oxidation. To assess effects on cellular protein of endogenous versus exogenous oxidative stress, a proteomics approach was used to compare disulfide bondcontaining proteins in the idp2Δzwf1Δ strain following shifts to acetate and oleate media with those in the parental strain following similar shifts to media containing hydrogen peroxide. Among prominent disulfide bond-containing proteins were several with known antioxidant functions. These and several other proteins were detected as multiple electrophoretic isoforms, with some isoforms containing disulfide bonds under all conditions and other isoforms exhibiting a redox-sensitive content of disulfide bonds, i.e., in the idp2Δzwf1Δ strain and in the hydrogen peroxide-challenged parental strain. The disulfide bond content of some isoforms of these proteins was also elevated in the parental strain grown on glucose, possibly suggesting a redirection of NADPH reducing equivalents to support rapid growth. Further examination of protein carbonylation in the idp2Δzwf1Δ strain shifted to oleate medium also led to identification of common and unique protein targets of endogenous oxidative stress.

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Section: Discussionsupporting

confidence: 61%

Section: Discussionmentioning

confidence: 95%

Section: Assays For Disulfide Bondsmentioning

confidence: 99%

Section: Specific Proteins Modified By Carbonylationmentioning

confidence: 99%

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Changes in disulfide bond content of proteins in a yeast strain lacking major sources of NADPH

Minard

Carroll

Weintraub

et al. 2007

Free Radical Biology and Medicine

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“…Protein oxidation was determined by immunodetection of protein carbonyls, as previous described (Costa et al, 2002). Protein content of cellular extracts was estimated by the method of Lowry, using bovine serum albumin as a standard.…”

Section: Protein Carbonylation Lipid Peroxidation and Intracellular mentioning

confidence: 99%

Isc1p Plays a Key Role in Hydrogen Peroxide Resistance and Chronological Lifespan through Modulation of Iron Levels and Apoptosis

Almeida

Marques

Mojžita

et al. 2008

MBoC

Self Cite

107

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The inositolphosphosphingolipid phospholipase C (Isc1p) of Saccharomyces cerevisiae belongs to the family of neutral sphingomyelinases that generates the bioactive sphingolipid ceramide. In this work the role of Isc1p in oxidative stress resistance and chronological lifespan was investigated. Loss of Isc1p resulted in a higher sensitivity to hydrogen peroxide that was associated with an increase in oxidative stress markers, namely intracellular oxidation, protein carbonylation, and lipid peroxidation. Microarray analysis showed that Isc1p deficiency up-regulated the iron regulon leading to increased levels of iron, which is known to catalyze the production of the highly reactive hydroxyl radicals via the Fenton reaction. In agreement, iron chelation suppressed hydrogen peroxide sensitivity of isc1⌬ mutants. Cells lacking Isc1p also displayed a shortened chronological lifespan associated with oxidative stress markers and aging of parental cells was correlated with a decrease in Isc1p activity. The analysis of DNA fragmentation and caspase-like activity showed that Isc1p deficiency increased apoptotic cell death associated with oxidative stress and aging. Furthermore, deletion of Yca1p metacaspase suppressed the oxidative stress sensitivity and premature aging phenotypes of isc1⌬ mutants. These results indicate that Isc1p plays an important role in the regulation of cellular redox homeostasis, through modulation of iron levels, and of apoptosis.

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Oxidative Damage to Proteins: Structural Modifications and Consequences in Cell Function

Cabiscol

Ros

2006

Redox Proteomics

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Hydrogen peroxide-induced carbonylation of key metabolic enzymes in Saccharomyces cerevisiae: the involvement of the oxidative stress response regulators Yap1 and Skn7

Cited by 135 publications

References 47 publications

Changes in disulfide bond content of proteins in a yeast strain lacking major sources of NADPH

Changes in disulfide bond content of proteins in a yeast strain lacking major sources of NADPH

Isc1p Plays a Key Role in Hydrogen Peroxide Resistance and Chronological Lifespan through Modulation of Iron Levels and Apoptosis

Oxidative Damage to Proteins: Structural Modifications and Consequences in Cell Function

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