Oxidative damage to proteins in yeast cells exposed to adaptive levels of H<sub>2</sub>O<sub>2</sub>

Poljak, Anne; Dawes, Ian W.; Ingelse, Benno; Duncan, Mark W.; Smythe, George A.; Grant, Chris M.

doi:10.1179/135100003225003401

Cited by 26 publications

(20 citation statements)

References 42 publications

(43 reference statements)

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“…Hydroxyl radical attack on the amino acid phenylalanine generates o- , m- and p- tyrosine were detected using gas chromatography/mass spectrometry (GC/MS) [44], [45]. Figure 1 shows the age-related changes in o - (Fig.…”

Section: Resultsmentioning

confidence: 99%

Age Related Changes in NAD+ Metabolism Oxidative Stress and Sirt1 Activity in Wistar Rats

et al. 2011

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The cofactor nicotinamide adenine dinucleotide (NAD+) has emerged as a key regulator of metabolism, stress resistance and longevity. Apart from its role as an important redox carrier, NAD+ also serves as the sole substrate for NAD-dependent enzymes, including poly(ADP-ribose) polymerase (PARP), an important DNA nick sensor, and NAD-dependent histone deacetylases, Sirtuins which play an important role in a wide variety of processes, including senescence, apoptosis, differentiation, and aging. We examined the effect of aging on intracellular NAD+ metabolism in the whole heart, lung, liver and kidney of female wistar rats. Our results are the first to show a significant decline in intracellular NAD+ levels and NAD∶NADH ratio in all organs by middle age (i.e.12 months) compared to young (i.e. 3 month old) rats. These changes in [NAD(H)] occurred in parallel with an increase in lipid peroxidation and protein carbonyls (o- and m- tyrosine) formation and decline in total antioxidant capacity in these organs. An age dependent increase in DNA damage (phosphorylated H2AX) was also observed in these same organs. Decreased Sirt1 activity and increased acetylated p53 were observed in organ tissues in parallel with the drop in NAD+ and moderate over-expression of Sirt1 protein. Reduced mitochondrial activity of complex I–IV was also observed in aging animals, impacting both redox status and ATP production. The strong positive correlation observed between DNA damage associated NAD+ depletion and Sirt1 activity suggests that adequate NAD+ concentrations may be an important longevity assurance factor.

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Section: Resultsmentioning

confidence: 99%

Age Related Changes in NAD+ Metabolism Oxidative Stress and Sirt1 Activity in Wistar Rats

et al. 2011

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“…Yeast pre-incubation with 0.5 mM hydrogen peroxide increased tolerance to 7.5 mM hydrogen peroxide for all yeast in this study (Figure 1E). Increased tolerance to hydrogen peroxide-induced oxidative stress under constant exposure has been reported previously for S. cerevisiae [32]. …”

Section: Resultssupporting

confidence: 55%

Tolerance of pentose utilising yeast to hydrogen peroxide-induced oxidative stress

et al. 2014

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BackgroundBioethanol fermentations follow traditional beverage fermentations where the yeast is exposed to adverse conditions such as oxidative stress. Lignocellulosic bioethanol fermentations involve the conversion of pentose and hexose sugars into ethanol. Environmental stress conditions such as osmotic stress and ethanol stress may affect the fermentation performance; however, oxidative stress as a consequence of metabolic output can also occur. However, the effect of oxidative stress on yeast with pentose utilising capabilities has yet to be investigated.ResultsAssaying for the effect of hydrogen peroxide-induced oxidative stress on Candida, Pichia and Scheffersomyces spp. has demonstrated that these yeast tolerate hydrogen peroxide-induced oxidative stress in a manner consistent with that demonstrated by Saccharomyces cerevisiae. Pichia guillermondii appears to be more tolerant to hydrogen peroxide-induced oxidative stress when compared to Candida shehatae, Candida succiphila or Scheffersomyces stipitis.ConclusionsSensitivity to hydrogen peroxide-induced oxidative stress increased in the presence of minimal media; however, addition of amino acids and nucleobases was observed to increase tolerance. In particular adenine increased tolerance and methionine reduced tolerance to hydrogen peroxide-induced oxidative stress.

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“…Free amino acids and amino acids in proteins are highly susceptible to oxidation by ROS (98). Oxidized amino acids can be detected in yeast cells; for example, oxidized phenylalanine (m-and o-Tyr) is elevated after exposure to similar concentrations of H 2 O 2 as those that activate Gcn2 (80). Although the levels of oxidized amino acids detected in yeast cells exposed to H 2 O 2 are relatively low, representing about one modification per 10 3 phenylalanine residues, the total oxidative load on the amino acid pool may trigger an amino acid starvation response.…”

Section: Grantmentioning

confidence: 99%

Regulation of Translation by Hydrogen Peroxide

Grant

2011

Antioxidants & Redox Signaling

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Cells must be able to maintain their intracellular homeostasis in the face of changing conditions. Typically, they respond by invoking complex regulatory mechanisms, including a global inhibition of translation. This reduction in protein synthesis may prevent continued gene expression during potentially error-prone conditions as well as allow for the turnover of existing mRNAs and proteins, whilst gene expression is directed toward the production of new molecules required to protect against or detoxify the stress. However, it is becoming increasingly recognized that not all translation is inhibited and translational control of specific mRNAs is required for survival under stress conditions. Control of protein levels via translational regulation offers a significant advantage to the cell due to the immediacy of the regulatory effect. This review describes how protein synthesis is regulated in response to oxidative stress conditions induced by exposure to hydrogen peroxide. Translational control can be mediated via direct oxidative regulation of translation factors as well via mRNA-specific regulatory mechanisms. Additionally, increasing evidence suggests that oxidative damage to the translational apparatus can itself alter the proteomic output. The resulting translational reprogramming is fundamental for adaptation to the oxidative stress.

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Oxidative damage to proteins in yeast cells exposed to adaptive levels of H₂O₂

Cited by 26 publications

References 42 publications

Age Related Changes in NAD+ Metabolism Oxidative Stress and Sirt1 Activity in Wistar Rats

Age Related Changes in NAD+ Metabolism Oxidative Stress and Sirt1 Activity in Wistar Rats

Tolerance of pentose utilising yeast to hydrogen peroxide-induced oxidative stress

Regulation of Translation by Hydrogen Peroxide

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Oxidative damage to proteins in yeast cells exposed to adaptive levels of H2O2

Cited by 26 publications

References 42 publications

Age Related Changes in NAD+ Metabolism Oxidative Stress and Sirt1 Activity in Wistar Rats

Age Related Changes in NAD+ Metabolism Oxidative Stress and Sirt1 Activity in Wistar Rats

Tolerance of pentose utilising yeast to hydrogen peroxide-induced oxidative stress

Regulation of Translation by Hydrogen Peroxide

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Oxidative damage to proteins in yeast cells exposed to adaptive levels of H₂O₂