Cytochrome <i>c</i> is released from coupled mitochondria of yeast en route to acetic acid‐induced programmed cell death and can work as an electron donor and a ROS scavenger

Giannattasio, Sergio; Atlante, Anna; Antonacci, Lucia; Guaragnella, Nicoletta; Lattanzio, Paolo; Passarella, Salvatore; Marra, Ersilia

doi:10.1016/j.febslet.2008.03.048

Cited by 55 publications

(65 citation statements)

References 33 publications

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“…It is widely believed that AA toxicity is associated with reactive oxygen species (ROS) generation and programmed cell death induction in the yeast. [8][9][10][11][12] To study and compare possible mechanisms of acetate and propionate effects on yeast, we monitored CP accumulation and the activities of selected antioxidant enzymes. These parameters are used as markers of oxidative stress.…”

Section: Discussionmentioning

confidence: 99%

“…[1][2][3][4][5][6] It was found that WOAs were mutagenic towards the mitochondrial genome in aerobically grown baker's yeast. 2 Accumulation of acid anions in the yeast cells also resulted in energetic stress, 7 programmed cell death, [8][9][10][11][12] and inhibition of essential metabolic pathways. [13][14][15] On the other hand, baker's yeast is shown to be relatively resistant to monocarboxylic WOAs.…”

Section: Introductionmentioning

confidence: 99%

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Acetate but not propionate induces oxidative stress in bakers’ yeastSaccharomyces cerevisiae

et al. 2011

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The influence of acetic and propionic acids on baker's yeast was investigated in order to expand our understanding of the effect of weak organic acid food preservatives on eukaryotic cells. Both acids decreased yeast survival in a concentration-dependent manner, but with different efficiencies. The acids inhibited the fluorescein efflux from yeast cells. The inhibition constant of fluorescein extrusion from cells treated with acetate was significantly lower in parental strain than in either PDR12 (ABC-transporter Pdr12p) or WAR1 (transcriptional factor of Pdr12p) defective mutants. The constants of inhibition by propionate were virtually the same in all strains used. Yeast exposure to acetate increased the level of oxidized proteins and the activity of antioxidant enzymes, while propionate did not change these parameters. This suggests that various mechanisms underlie the yeast toxicity by acetic and propionic acids. Our studies with mutant cells clearly indicated the involvement of Yap1p transcriptional regulator and de novo protein synthesis in superoxide dismutase up-regulation by acetate. The up-regulation of catalase was Yap1p independent. Yeast pre-incubation with low concentrations of H 2 O 2 caused cellular cross-protection against high concentrations of acetate. The results are discussed from the point of view that acetate induces a prooxidant effect in vivo, whereas propionate does not.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Acetate but not propionate induces oxidative stress in bakers’ yeastSaccharomyces cerevisiae

et al. 2011

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“…Unlike cyt c from higher eukaryotes, the release of yeast cyt c (y-cyt c) does not activate caspases (36). Instead, the concentration of y-cyt c, once it appears in the cytosol diminishes with time (37). The mechanism of the absence of pro-apoptotic activity of the released y-cyt c in the yeast, and the observed reduction of the concentration of released y-cyt c with time is not yet understood completely.…”

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confidence: 99%

Subtle Change in the Charge Distribution of Surface Residues May Affect the Secondary Functions of Cytochrome c

Paul¹,

Sil²,

Haldar³

et al. 2015

Journal of Biological Chemistry

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Background:The cardiolipin (CDL) binding and the peroxidase activity of cytochrome c (cyt c) vary with the protein source. Results: The CDL binding and the peroxidase activity of cyt c depend on conformational heterogeneity and oligomerization. Conclusion: Subtle variations in the surface residues of cyt c influence its conformational dynamics and stability. Significance: Secondary functions of cyt c have been studied at single-molecule resolution.

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“…Even though a function for cytosolic Cc during PCD has been defined only in mammals (8), the mitochondria-to-cytoplasm release of Cc is an evolutionarily conserved event found to occur in yeast (17), plants (18), flies (19), and mammals (20).…”

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confidence: 99%

Structural and Functional Analysis of Novel Human Cytochrome c Targets in Apoptosis

Martínez-Fábregas

Dı́az-Moreno

González‐Arzola

et al. 2014

Molecular & Cellular Proteomics

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Since the first description of apoptosis four decades ago, great efforts have been made to elucidate, both in vivo and in vitro, the molecular mechanisms involved in its regulation. Although the role of cytochrome c during apoptosis is well established, relatively little is known about its participation in signaling pathways in vivo due to its essential role during respiration. To obtain a better understanding of the role of cytochrome c in the onset of apoptosis, we used a proteomic approach based on affinity chromatography with cytochrome c as bait in this study. In this approach, novel cytochrome c interaction partners were identified whose in vivo interaction and cellular localization were facilitated through bimolecular fluorescence complementation. Modeling of the complex interface between cytochrome c and its counterparts indicated the involvement of the surface surrounding the heme crevice of cytochrome c, in agreement with the vast majority of known redox adducts of cytochrome c. However, in contrast to the high turnover rate of the mitochondrial cytochrome c redox adducts, those occurring under apoptosis led to the formation of stable nucleo-cytoplasmic ensembles, as inferred mainly from surface plasmon resonance and nuclear magnetic resonance measurements, which permitted us to corroborate the formation of such complexes in vitro. The results obtained suggest that human cytochrome c interacts with pro-survival, anti-apoptotic proteins following its release into the cytoplasm. Thus, cytochrome c may interfere with cell survival pathways and unlock apoptosis in order to prevent the spatial and temporal coexistence of antagonist signals. Molecular & Cellular

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Cytochrome c is released from coupled mitochondria of yeast en route to acetic acid‐induced programmed cell death and can work as an electron donor and a ROS scavenger

Cited by 55 publications

References 33 publications

Acetate but not propionate induces oxidative stress in bakers’ yeastSaccharomyces cerevisiae

Acetate but not propionate induces oxidative stress in bakers’ yeastSaccharomyces cerevisiae

Subtle Change in the Charge Distribution of Surface Residues May Affect the Secondary Functions of Cytochrome c

Structural and Functional Analysis of Novel Human Cytochrome c Targets in Apoptosis

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