Journal articles: 'Yeast apoptosis'

1

Reiter, Jochen, Eva Herker, Frank Madeo, and Manfred J. Schmitt. "Viral killer toxins induce caspase-mediated apoptosis in yeast." Journal of Cell Biology 168, no. 3 (January 24, 2005): 353–58. http://dx.doi.org/10.1083/jcb.200408071.

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In yeast, apoptotic cell death can be triggered by various factors such as H2O2, cell aging, or acetic acid. Yeast caspase (Yca1p) and cellular reactive oxygen species (ROS) are key regulators of this process. Here, we show that moderate doses of three virally encoded killer toxins (K1, K28, and zygocin) induce an apoptotic yeast cell response, although all three toxins differ significantly in their primary killing mechanisms. In contrast, high toxin concentrations prevent the occurrence of an apoptotic cell response and rather cause necrotic, toxin-specific cell killing. Studies with Δyca1 and Δgsh1 deletion mutants indicate that ROS accumulation as well as the presence of yeast caspase 1 is needed for apoptosis in toxin-treated yeast cells. We conclude that in the natural environment of toxin-secreting killer yeasts, where toxin concentration is usually low, induction of apoptosis might play an important role in efficient toxin-mediated cell killing.

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Wissing, Silke, Paula Ludovico, Eva Herker, Sabrina Büttner, Silvia M. Engelhardt, Thorsten Decker, Alexander Link, et al. "An AIF orthologue regulates apoptosis in yeast." Journal of Cell Biology 166, no. 7 (September 20, 2004): 969–74. http://dx.doi.org/10.1083/jcb.200404138.

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Apoptosis-inducing factor (AIF), a key regulator of cell death, is essential for normal mammalian development and participates in pathological apoptosis. The proapoptotic nature of AIF and its mode of action are controversial. Here, we show that the yeast AIF homologue Ynr074cp controls yeast apoptosis. Similar to mammalian AIF, Ynr074cp is located in mitochondria and translocates to the nucleus of yeast cells in response to apoptotic stimuli. Purified Ynr074cp degrades yeast nuclei and plasmid DNA. YNR074C disruption rescues yeast cells from oxygen stress and delays age-induced apoptosis. Conversely, overexpression of Ynr074cp strongly stimulates apoptotic cell death induced by hydrogen peroxide and this effect is attenuated by disruption of cyclophilin A or the yeast caspase YCA1. We conclude that Ynr074cp is a cell death effector in yeast and rename it AIF-1 (Aif1p, gene AIF1).

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Madeo, Frank, Eleonore Fröhlich, Martin Ligr, Martin Grey, Stephan J. Sigrist, Dieter H. Wolf, and Kai-Uwe Fröhlich. "Oxygen Stress: A Regulator of Apoptosis in Yeast." Journal of Cell Biology 145, no. 4 (May 17, 1999): 757–67. http://dx.doi.org/10.1083/jcb.145.4.757.

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Oxygen radicals are important components of metazoan apoptosis. We have found that apoptosis can be induced in the yeast Saccharomyces cerevisiae by depletion of glutathione or by low external doses of H2O2. Cycloheximide prevents apoptotic death revealing active participation of the cell. Yeast can also be triggered into apoptosis by a mutation in CDC48 or by expression of mammalian bax. In both cases, we show oxygen radicals to accumulate in the cell, whereas radical depletion or hypoxia prevents apoptosis. These results suggest that the generation of oxygen radicals is a key event in the ancestral apoptotic pathway and offer an explanation for the mechanism of bax-induced apoptosis in the absence of any established apoptotic gene in yeast.

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Jin, Can, and John C. Reed. "Yeast and apoptosis." Nature Reviews Molecular Cell Biology 3, no. 6 (June 2002): 453–59. http://dx.doi.org/10.1038/nrm832.

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Madeo, Frank, Eva Herker, Silke Wissing, Helmut Jungwirth, Tobias Eisenberg, and Kai-Uwe Fröhlich. "Apoptosis in yeast." Current Opinion in Microbiology 7, no. 6 (December 2004): 655–60. http://dx.doi.org/10.1016/j.mib.2004.10.012.

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Herker, Eva, Helmut Jungwirth, Katharina A. Lehmann, Corinna Maldener, Kai-Uwe Fröhlich, Silke Wissing, Sabrina Büttner, Markus Fehr, Stephan Sigrist, and Frank Madeo. "Chronological aging leads to apoptosis in yeast." Journal of Cell Biology 164, no. 4 (February 16, 2004): 501–7. http://dx.doi.org/10.1083/jcb.200310014.

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During the past years, yeast has been successfully established as a model to study mechanisms of apoptotic regulation. However, the beneficial effects of such a cell suicide program for a unicellular organism remained obscure. Here, we demonstrate that chronologically aged yeast cultures die exhibiting typical markers of apoptosis, accumulate oxygen radicals, and show caspase activation. Age-induced cell death is strongly delayed by overexpressing YAP1, a key transcriptional regulator in oxygen stress response. Disruption of apoptosis through deletion of yeast caspase YCA1 initially results in better survival of aged cultures. However, surviving cells lose the ability of regrowth, indicating that predamaged cells accumulate in the absence of apoptotic cell removal. Moreover, wild-type cells outlast yca1 disruptants in direct competition assays during long-term aging. We suggest that apoptosis in yeast confers a selective advantage for this unicellular organism, and demonstrate that old yeast cells release substances into the medium that stimulate survival of the clone.

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Liang, Qiuli, and Bing Zhou. "Copper and Manganese Induce Yeast Apoptosis via Different Pathways." Molecular Biology of the Cell 18, no. 12 (December 2007): 4741–49. http://dx.doi.org/10.1091/mbc.e07-05-0431.

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Metal ions are essential as well as toxic to the cell. The mechanism of metal-induced toxicity is not well established. Here, for the first time we studied two essential nutritional elements, copper and manganese, for their apoptotic effects in yeast Saccharomyces cerevisiae. Although beneficial at subtoxic levels, we demonstrated that at moderately toxic levels, both metals induce extensive apoptosis in yeast cells. At even higher concentrations, necrosis takes over. Furthermore, we investigated the molecular pathways mediating Cu- and Mn-mediated apoptotic action. Mitochondria-defective yeast exhibit a much reduced apoptotic marker expression and better survival under Cu and Mn stress, indicating mitochondria are involved in both Cu- and Mn-induced apoptosis. Reactive oxygen species (ROS) are generated in high amounts in Cu- but not in Mn-induced cell death, and Cu toxicity can be alleviated by overexpression of superoxide dismutase 2, suggesting ROS mediate Cu but not Mn toxicity. Yeast metacaspase Yca1p is not involved in Cu-induced apoptosis, although it plays an important role in the Mn-induced process. A genetic screen identified Cpr3p, a yeast cyclophilin D homologue, as mediating the Cu-induced apoptotic program. Cpr3p mutant seems to eliminate Cu-induced apoptosis without affecting ROS production, while leaving necrosis intact. These results may provide important insight into a detailed understanding at the molecular and cellular level of metal toxicity and metal accumulation diseases.

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8

LeBrasseur, Nicole. "Yeast apoptosis debate continues." Journal of Cell Biology 166, no. 7 (September 27, 2004): 938. http://dx.doi.org/10.1083/jcb1667iti1.

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9

Schmitt, Manfred J., and Jochen Reiter. "Viral induced yeast apoptosis." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1783, no. 7 (July 2008): 1413–17. http://dx.doi.org/10.1016/j.bbamcr.2008.01.017.

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10

Sousa, Maria João, Flávìa Azevedo, Ana Pedras, Carolina Marques, Olga P. Coutinho, Ana Preto, Hernâni Gerós, Susana R. Chaves, and Manuela Côrte-Real. "Vacuole–mitochondrial cross-talk during apoptosis in yeast: a model for understanding lysosome–mitochondria-mediated apoptosis in mammals." Biochemical Society Transactions 39, no. 5 (September 21, 2011): 1533–37. http://dx.doi.org/10.1042/bst0391533.

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The yeast apoptosis field emerged with the finding that key components of the apoptotic machinery are conserved in these simple eukaryotes. Thus it became possible to exploit these genetically tractable organisms to improve our understanding of the intricate mechanisms of cell death in higher eukaryotes and of severe human diseases associated with apoptosis dysfunctions. Early on, it was recognized that a mitochondria-mediated apoptotic pathway showing similarities to the mammalian intrinsic pathway was conserved in yeast. Recently, lysosomes have also emerged as central players in mammalian apoptosis. Following LMP (lysosomal membrane permeabilization), lysosomal proteases such as cathepsins B, D and L are released into the cytosol and can trigger a mitochondrial apoptotic cascade. CatD (cathepsin D) can also have anti-apoptotic effects in some cellular types and specific contexts. Nonetheless, the mechanisms underlying LMP and the specific role of cathepsins after their release into the cytosol remain poorly understood. We have recently shown that yeast vacuoles, membrane-bound acidic organelles, which share many similarities to plant vacuoles and mammalian lysosomes, are also involved in the regulation of apoptosis and that the vacuolar protease Pep4p, orthologue of the human CatD, is released from the vacuole into the cytosol in response to acetic acid. Here, we discuss how the conservation of cell-death regulation mechanisms in yeast by the lysosome-like organelle and mitochondria may provide new insights into the understanding of the complex interplay between the mitochondria and lysosome-mediated signalling routes during mammalian apoptosis.

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11

Rajan, Teena, Benluvankar V, and Vincent S. "SACCHAROMYCES CEREVISIAE-INDUCED APOPTOSIS OF MONOLAYER CERVICAL CANCER CELLS." Asian Journal of Pharmaceutical and Clinical Research 10, no. 8 (August 1, 2017): 63. http://dx.doi.org/10.22159/ajpcr.2017.v10i8.18818.

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Objective: The present study was undertaken to examine the effect of phagocytosis of killed yeast on the induction of apoptosis in monolayer of HeLa cells.Methods: HeLa cell line was incubated with different doses (1000-7.8 μg/ml) of heat-killed Saccharomyces cerevisiae for 24, 48, and 72 hrs. The cytotoxicity against HeLa cell line during different exposure hours was screened by 3-(4, 5-dimethyl-2-thiazolyl)-2, 5-diphenyl-tetrazolium bromide assay. Induction of apoptosis was further confirmed by morphological and biochemical examination. Antiproliferative effect of yeast was examined under inverted microscope. Cell morphological changes were analyzed by fluorescent staining with propidium iodide.Results: The results showed that yeast induces cytotoxicity against HeLa cells in concentrations and during prolonged exposure periods. The viability of HeLa cells decreased from 85% to 45% during 72 hrs of treatment with 1000 μg/ml of yeast cells. The inhibitory concentration 50% of heat-killed yeast required to induce 50% inhibition of HeLa cells was 62.5 μg/ml. Apoptotic cells showed signs such as cell enlargement, membrane blebbing, and chromatin condensation. Furthermore, cell cycle analysis showed that S. cerevisiae treated HeLa cells and showed a typical apoptosis pattern of DNA content that reflected sub-G0 phase (corresponding to apoptotic cells).Conclusion: Results from the present work show that the heat-killed yeast has anticancer activity and it includes apoptosis of HeLa cells in vitro.

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12

Pentz, Jennifer T., Bradford P. Taylor, and William C. Ratcliff. "Apoptosis in snowflake yeast: novel trait, or side effect of toxic waste?" Journal of The Royal Society Interface 13, no. 118 (May 2016): 20160121. http://dx.doi.org/10.1098/rsif.2016.0121.

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Recent experiments evolving de novo multicellularity in yeast have found that large cluster-forming genotypes also exhibit higher rates of programmed cell death (apoptosis). This was previously interpreted as the evolution of a simple form of cellular division of labour: apoptosis results in the scission of cell–cell connections, allowing snowflake yeast to produce proportionally smaller, faster-growing propagules. Through spatial simulations, Duran-Nebreda and Solé ( J. R. Soc. Interface 12, 20140982 ( doi:10.1073/pnas.1115323109 )) develop the novel null hypothesis that apoptosis is not an adaptation, per se , but is instead caused by the accumulation of toxic metabolites in large clusters. Here we test this hypothesis by synthetically creating unicellular derivatives of snowflake yeast through functional complementation with the ancestral ACE2 allele. We find that multicellular snowflake yeast with elevated apoptosis exhibit a similar rate of apoptosis when cultured as single cells. We also show that larger snowflake yeast clusters tend to contain a greater fraction of older, senescent cells, which may explain why larger clusters of a given genotype are more apoptotic. Our results show that apoptosis is not caused by side effects of spatial structure, such as starvation or waste product accumulation, and are consistent with the hypothesis that elevated apoptosis is a trait that co-evolves with large cluster size.

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13

Polčic, Peter, Lucia Pakosová, Petra Chovančíková, and Zdenko Machala. "Reactive cold plasma particles generate oxidative stress in yeast but do not trigger apoptosis." Canadian Journal of Microbiology 64, no. 6 (June 2018): 367–75. http://dx.doi.org/10.1139/cjm-2017-0753.

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Interactions of living cells with cold plasma of electrical discharges affect cell physiology, often resulting in the loss of viability. However, the mechanisms involved in cell killing are poorly understood, and dissection of cellular pathways or structures affected by plasma using simple eukaryotic models is needed. Using selected genetic mutants of yeast (Saccharomyces cerevisiae), we investigated the role of oxidative stress and yeast apoptosis in plasma-induced cell killing. Increased sensitivity of yeast strains deficient in superoxide dismutases indicated that reactive oxygen species generated in the plasma are among the most prominent factors involved in killing of yeast cells. In mutant strains with a deletion of the key components of yeast apoptotic pathway, the sensitivity of cells towards the plasma treatment remained unaffected. Yeast apoptosis, thus, does not appear to play a significant role in plasma-induced cell killing of yeast.

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Porras-Agüera, Moreno-García, Mauricio, Moreno, and García-Martínez. "First Proteomic Approach to Identify Cell Death Biomarkers in Wine Yeasts during Sparkling Wine Production." Microorganisms 7, no. 11 (November 8, 2019): 542. http://dx.doi.org/10.3390/microorganisms7110542.

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Apoptosis and later autolysis are biological processes which take place in Saccharomyces cerevisiae during industrial fermentation processes, which involve costly and time-consuming aging periods. Therefore, the identification of potential cell death biomarkers can contribute to the creation of a long-term strategy in order to improve and accelerate the winemaking process. Here, we performed a proteomic analysis based on the detection of possible apoptosis and autolysis protein biomarkers in two industrial yeast strains commonly used in post-fermentative processes (sparkling wine secondary fermentation and biological aging) under typical sparkling wine elaboration conditions. Pressure had a negatively effect on viability for flor yeast, whereas the sparkling wine strain seems to be more adapted to these conditions. Flor yeast strain experienced an increase in content of apoptosis-related proteins, glucanases and vacuolar proteases at the first month of aging. Significant correlations between viability and apoptosis proteins were established in both yeast strains. Multivariate analysis based on the proteome of each process allowed to distinguish among samples and strains. The proteomic profile obtained in this study could provide useful information on the selection of wine strains and yeast behavior during sparkling wine elaboration. Additionally, the use of flor yeasts for sparkling wine improvement and elaboration is proposed.

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15

Almeida, B., S. Buttner, S. Ohlmeier, A. Silva, A. Mesquita, B. Sampaio-Marques, N. S. Osorio, et al. "NO-mediated apoptosis in yeast." Journal of Cell Science 120, no. 18 (August 28, 2007): 3279–88. http://dx.doi.org/10.1242/jcs.010926.

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16

Almeida, B., A. Silva, A. Mesquita, B. Sampaio-Marques, F. Rodrigues, and P. Ludovico. "Drug-induced apoptosis in yeast." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1783, no. 7 (July 2008): 1436–48. http://dx.doi.org/10.1016/j.bbamcr.2008.01.005.

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17

Leadsham, Jane E., and Campbell W. Gourlay. "Cytoskeletal induced apoptosis in yeast." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1783, no. 7 (July 2008): 1406–12. http://dx.doi.org/10.1016/j.bbamcr.2008.01.019.

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Mazzoni, Cristina, and Claudio Falcone. "Caspase-dependent apoptosis in yeast." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1783, no. 7 (July 2008): 1320–27. http://dx.doi.org/10.1016/j.bbamcr.2008.02.015.

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Liang, Qiuli, Wei Li, and Bing Zhou. "Caspase-independent apoptosis in yeast." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1783, no. 7 (July 2008): 1311–19. http://dx.doi.org/10.1016/j.bbamcr.2008.02.018.

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20

Pereira, C., R. D. Silva, L. Saraiva, B. Johansson, M. J. Sousa, and M. Côrte-Real. "Mitochondria-dependent apoptosis in yeast." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1783, no. 7 (July 2008): 1286–302. http://dx.doi.org/10.1016/j.bbamcr.2008.03.010.

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Emami, Parvaneh, and Masaru Ueno. "3,3’-Diindolylmethane induces apoptosis and autophagy in fission yeast." PLOS ONE 16, no. 12 (December 10, 2021): e0255758. http://dx.doi.org/10.1371/journal.pone.0255758.

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3,3’-Diindolylmethane (DIM) is a compound derived from the digestion of indole-3-carbinol, found in the broccoli family. It induces apoptosis and autophagy in some types of human cancer. DIM extends lifespan in the fission yeast Schizosaccharomyces pombe. The mechanisms by which DIM induces apoptosis and autophagy in humans and expands lifespan in fission yeasts are not fully understood. Here, we show that DIM induces apoptosis and autophagy in log-phase cells, which is dose-dependent in fission yeast. A high concentration of DIM disrupted the nuclear envelope (NE) structure and induced chromosome condensation at an early time point. In contrast, a low concentration of DIM induced autophagy but did not disrupt NE structure. The mutant defective in autophagy was more sensitive to a low concentration of DIM, demonstrating that the autophagic pathway contributes to the survival of cells against DIM. Moreover, our results showed that the lem2 mutant is more sensitive to DIM. NE in the lem2 mutant was disrupted even at the low concentration of DIM. Our results demonstrate that the autophagic pathway and NE integrity are important to maintain viability in the presence of a low concentration of DIM. The mechanism of apoptosis and autophagy induction by DIM might be conserved in fission yeast and humans. Further studies will contribute to the understanding of the mechanism of apoptosis and autophagy by DIM in fission yeast and humans.

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Cristofolini, A., C. Merkis, M. Fiorimanti, A. Magnoli, M. Caverzan, and L. Cavaglieri. "Saccharomyces cerevisiae RC016 modulates the apoptotic pathways in rat livers treated with aflatoxin B1." World Mycotoxin Journal 12, no. 4 (December 4, 2019): 387–97. http://dx.doi.org/10.3920/wmj2019.2472.

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The aim was to study the effect of probiotic Saccharomyces cerevisiae RC016 on the expression of apoptotic protein Bax, Bcl-2, DR4 and c-FLIP, in liver of rats exposed to aflatoxin B1 (AFB1). Four treatments were applied to inbred male Wistar rats: uncontaminated feed control, S. cerevisiae RC016 control, contaminated feed with 100 μg/kg AFB1 and contaminated feed with 100 μg/kg AFB1 + daily oral dose 108 viable S. cerevisiae RC016 cells. Histological technique and high-resolution light microscopy (HRLM) were performed to the study of tissue morphology, the TUNEL assay was used to determine the apoptosis cellular and the expression of Bax, Bcl-2, DR4 and c-FLIP was determinate through immunohistochemistry. In liver the necrotic lesions observed with AFB1 treatment were reduced with the addition of yeast. The highest apoptotic index (IAp) was found in the yeast control, with AFB1 decrease significantly the IAp, while with the addition of yeast increase the IAp of liver cells. This was confirmed by HRLM. DR4 receptor was not present in any of the treatments. The immunolabeling of c-FLIP showed a statistically significant increase in the treatments with S. cerevisiae. The extrinsic pathway of apoptosis through the FAS-receptors would neither be active in the apoptotic process observed in rat livers in the treatments with yeast. Significant differences between proteins Bax and Bcl-2 and effect of treatments on the immunolabeling of Bax were determinate. The exposure to AFB1 decreased the IAp in the livers; while the addition of the yeast produced a significant statistically increase of IAp. In this study it was determined that the apoptosis in liver would be induced by the intrinsic pathway through Bax. These suggest that the incorporation of the autocrine strain S. cerevisiae RC016 increases the apoptosis in liver, counteracting the adverse effect of aflatoxin B1 and favouring the tissue remodulation.

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Akintade, Damilare D., and Bhabatosh Chaudhuri. "Identification of proteins involved in transcription/translation (eEF 1A1) as an inhibitor of Bax induced apoptosis." Molecular Biology Reports 47, no. 9 (September 2020): 6785–92. http://dx.doi.org/10.1007/s11033-020-05736-5.

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Abstract Eukaryotic elongation factor 1A1 (eEF1A1) is central to translational activity. It is involved in complexes that form signal transduction with protein kinase C, as well as being a signal transducer and activator of transcription 3. eEF1A1 and eEF1A2 are isoforms of the alpha subunit of elongating factor 1 complex. It has been reported that eEF1A1 is expressed in most human tissues but the brain, skeletal muscle and heart. eEF1A1 has been linked to both apoptosis and anti-apoptotic activities. In this study, eEF1A1 was co-expressed with Bax, a proapoptotic protein via heterologous expression of recombinant DNA in yeast cells. Assays were carried out to monitor the fate and state of yeast cells when eEF1A1 was co-expressed with Bax. The yeast strain (bearing an integrated copy of the Bax gene) was transformed with an episomal 2-micron plasmid that encodes HA-tagged eEF1A1 gene. The resultant strain would allow co-expression of Bax and eEF1A1 in yeast cells, Bax being under the control of the GAL1 promoter, while the PGK1 promoter drives eEF1A1 expression. Bcl 2A1, a known anti-apoptotic protein, was also co-expressed with Bax in yeast cells as a positive control, to study the anti-apoptotic characteristic of eEF-1A1. The part eEF1A1 plays in apoptosis has been contentious, amidst the pro and anti-apoptotic properties of eEF1A1, it was shown clearly, in this study that eEF1A1 portrays only anti-apoptotic property in the presence of pro-apoptotic protein, Bax.

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Badr El-Din, Nariman K., Ashraf Z. Mahmoud, Tahia Ali Hassan, and Mamdooh Ghoneum. "Baker’s Yeast Sensitizes Metastatic Breast Cancer Cells to Paclitaxel In Vitro." Integrative Cancer Therapies 17, no. 2 (November 21, 2017): 542–50. http://dx.doi.org/10.1177/1534735417740630.

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Our earlier studies have demonstrated that phagocytosis of baker’s yeast ( Saccharomyces cerevisiae) induces apoptosis in different cancer cell lines in vitro and in vivo. This study aimed to examine how baker’s yeast sensitizes murine and human breast cancer cells (BCC) to paclitaxel in vitro. This sensitizing effect makes lower concentrations of chemotherapy more effective at killing cancer cells, thereby enhancing the capacity of treatment. Three BCC lines were used: the metastatic murine 4T1 line, the murine Ehrlich ascites carcinoma (EAC) line, and the human breast cancer MCF-7 line. Cells were cultured with different concentrations of paclitaxel in the presence or absence of baker’s yeast. Cell survival and the IC50 values were determined by MTT assay and trypan blue exclusion method. Percent of DNA damage, apoptosis, and cell proliferation were examined by flow cytometry. Yeast alone and paclitaxel alone significantly decreased 4T1 cell viability postculture (24 and 48 hours), caused DNA damage, increased apoptosis, and suppressed cell proliferation. Baker’s yeast in the presence of paclitaxel increased the sensitivity of 4T1 cells to chemotherapy and caused effects that were greater than either treatment alone. The chemosensitizing effect of yeast was also observed with murine EAC cells and human MCF-7 cells, but to a lesser extent. These data suggest that dietary baker’s yeast is an effective chemosensitizer and can enhance the apoptotic capacity of paclitaxel against breast cancer cells in vitro. Baker’s yeast may represent a novel adjuvant for chemotherapy treatment.

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Yang, Hui, Qun Ren, and Zhaojie Zhang. "Cleavage of Mcd1 by Caspase-like Protease Esp1 Promotes Apoptosis in Budding Yeast." Molecular Biology of the Cell 19, no. 5 (May 2008): 2127–34. http://dx.doi.org/10.1091/mbc.e07-11-1113.

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Over the last decade, yeast has been used successfully as a model system for studying the molecular mechanism of apoptotic cell death. Here, we report that Mcd1, the yeast homology of human cohesin Rad21, plays an important role in hydrogen peroxide-induced apoptosis in yeast. On induction of cell death, Mcd1 is cleaved and the C-terminal fragment is translocated from nucleus into mitochondria, causing the decrease of mitochondrial membrane potential and the amplification of cell death in a cytochrome c-dependent manner. We further demonstrate that the caspase-like protease Esp1 has dual functions and that it is responsible for the cleavage of Mcd1 during the hydrogen peroxide-induced apoptosis. When apoptosis is induced, Esp1 is released from the anaphase inhibitor Pds1. The activated Esp1 acts as caspase-like protease for the cleavage of Mcd1, which enhances the cell death via its translocation from nucleus to mitochondria.

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Matangkasombut, Oranart, Roongtiwa Wattanawaraporn, Keiko Tsuruda, Masaru Ohara, Motoyuki Sugai, and Skorn Mongkolsuk. "Cytolethal Distending Toxin from Aggregatibacter actinomycetemcomitans Induces DNA Damage, S/G2 Cell Cycle Arrest, and Caspase- Independent Death in a Saccharomyces cerevisiae Model." Infection and Immunity 78, no. 2 (December 7, 2009): 783–92. http://dx.doi.org/10.1128/iai.00857-09.

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ABSTRACT Cytolethal distending toxin (CDT) is a bacterial toxin that induces G2/M cell cycle arrest, cell distension, and/or apoptosis in mammalian cells. It is produced by several Gram-negative species and may contribute to their pathogenicity. The catalytic subunit CdtB has homology with DNase I and may act as a genotoxin. However, the mechanism by which CdtB leads to cell death is not yet clearly understood. Here, we used Saccharomyces cerevisiae as a model to study the molecular pathways involved in the function of CdtB from Aggregatibacter actinomycetemcomitans, a cause of aggressive periodontitis. We show that A. actinomycetemcomitans CdtB (AaCdtB) expression induces S/G2 arrest and death in a DNase-catalytic residue and nuclear localization-dependent manner in haploid yeasts. Yeast strains defective in homologous recombination (HR) repair, but not other DNA repair pathways, are hypersensitive to AaCdtB, suggesting that HR is required for survival upon CdtB expression. In addition, yeast does not harbor the substrate for the other activity proposed for CdtB function, which is phosphatidylinositol-3,4,5-triphosphate phosphatase. Thus, these results suggest that direct DNA-damaging activity alone is sufficient for CdtB toxicity. To investigate how CdtB induces cell death, we examined the effect of CdtB in yeast strains with mutations in apoptotic regulators. Our results suggest that yeast death occurs independently of the yeast metacaspase gene YCA1 and the apoptosis-inducing factor AIF1 but is partially dependent on histone H2B serine 10 phosphorylation. Therefore, we report here the evidence that AaCdtB causes DNA damage that leads to nonapoptotic death in yeast and the first mutation that confers resistance to CdtB.

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Mihoubi, Wafa, Emna Sahli, Fatma Rezgui, Najeh Dabebi, Rabiaa Sayehi, Hajer Hassairi, Najla Masmoudi-Fourati, et al. "Whole and Purified Aqueous Extracts of Nigella sativa L. Seeds Attenuate Apoptosis and the Overproduction of Reactive Oxygen Species Triggered by p53 Over-Expression in the Yeast Saccharomyces cerevisiae." Cells 11, no. 5 (March 3, 2022): 869. http://dx.doi.org/10.3390/cells11050869.

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Plants are an important source of pharmacologically active compounds. In the present work, we characterize the impact of black cumin (Nigella sativa L.) aqueous extracts on a yeast model of p53-dependent apoptosis. To this end, the Saccharomyces cerevisiae recombinant strain over-expressing p53 was used. The over-expression of p53 triggers the expression of apoptotic markers: the externalization of phosphatidylserine, mitochondrial defect associated with cytochrome-c release and the induction of DNA strand breaks. These different effects were attenuated by Nigella sativa L. aqueous extracts, whereas these extracts have no effect on the level of p53 expression. Thus, we focus on the anti-apoptotic molecules present in the aqueous extract of Nigella sativa L. These extracts were purified and characterized by complementary chromatographic methods. Specific fluorescent probes were used to determine the effect of the extracts on yeast apoptosis. Yeast cells over-expressing p53 decrease in relative size and have lower mitochondrial content. The decrease in cell size was proportional to the decrease in mitochondrial content and of mitochondrial membrane potential (ΔΨm). These effects were prevented by the purified aqueous fraction obtained by fractionation with different columns, named C4 fraction. Yeast cell death was also characterized by reactive oxygen species (ROS) overproduction. In the presence of the C4 fraction, ROS overproduction was strongly reduced. We also noted that the C4 fraction promotes the cell growth of control yeast cells, which do not express p53, supporting the fact that this purified extract acts on cellular mediators activating cell proliferation independently of p53. Altogether, our data obtained on yeast cells over-expressing p53 demonstrate that anti-apoptotic molecules targeting p53-induced apoptosis associated with mitochondrial dysfunction and ROS overproduction are present in the aqueous extracts of Nigella seeds and in the purified aqueous C4 fraction.

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Leadsham, J. E., V. N. Kotiadis, D. J. Tarrant, and C. W. Gourlay. "Apoptosis and the yeast actin cytoskeleton." Cell Death & Differentiation 17, no. 5 (December 18, 2009): 754–62. http://dx.doi.org/10.1038/cdd.2009.196.

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Carmona-Gutierrez, D., T. Eisenberg, S. Büttner, C. Meisinger, G. Kroemer, and F. Madeo. "Apoptosis in yeast: triggers, pathways, subroutines." Cell Death & Differentiation 17, no. 5 (January 15, 2010): 763–73. http://dx.doi.org/10.1038/cdd.2009.219.

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GRANOT, D., A. LEVINE, and E. DORHEFETZ. "Sugar-induced apoptosis in yeast cells." FEMS Yeast Research 4, no. 1 (October 2003): 7–13. http://dx.doi.org/10.1016/s1567-1356(03)00154-5.

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Fraser, A. "Fermenting debate: do yeast undergo apoptosis?" Trends in Cell Biology 8, no. 6 (June 1, 1998): 219–21. http://dx.doi.org/10.1016/s0962-8924(98)01275-6.

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Fröhlich, Kai-Uwe, Heike Fussi, and Christoph Ruckenstuhl. "Yeast apoptosis—From genes to pathways." Seminars in Cancer Biology 17, no. 2 (April 2007): 112–21. http://dx.doi.org/10.1016/j.semcancer.2006.11.006.

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Perrone, Gabriel G., Shi-Xiong Tan, and Ian W. Dawes. "Reactive oxygen species and yeast apoptosis." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1783, no. 7 (July 2008): 1354–68. http://dx.doi.org/10.1016/j.bbamcr.2008.01.023.

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Owsianowski, Esther, David Walter, and Birthe Fahrenkrog. "Negative regulation of apoptosis in yeast." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1783, no. 7 (July 2008): 1303–10. http://dx.doi.org/10.1016/j.bbamcr.2008.03.006.

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Fabrizio, Paola, and Valter D. Longo. "Chronological aging-induced apoptosis in yeast." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1783, no. 7 (July 2008): 1280–85. http://dx.doi.org/10.1016/j.bbamcr.2008.03.017.

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Eisenberg, Tobias, Sabrina Büttner, Guido Kroemer, and Frank Madeo. "The mitochondrial pathway in yeast apoptosis." Apoptosis 12, no. 5 (February 9, 2007): 1011–23. http://dx.doi.org/10.1007/s10495-007-0758-0.

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Li, Wei, Libo Sun, Qiuli Liang, Juan Wang, Weike Mo, and Bing Zhou. "Yeast AMID Homologue Ndi1p Displays Respiration-restricted Apoptotic Activity and Is Involved in Chronological Aging." Molecular Biology of the Cell 17, no. 4 (April 2006): 1802–11. http://dx.doi.org/10.1091/mbc.e05-04-0333.

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Apoptosis-inducing factor (AIF) and AIF-homologous mitochondrion-associated inducer of death (AMID) are both mitochondrial flavoproteins that trigger caspase-independent apoptosis. Phylogenetic analysis suggests that these two proteins evolutionarily diverge back from their common prokaryote ancestor. Compared with AIF, the proapoptotic nature of AMID and its mode of action are much less clarified. Here, we show that overexpression of yeast AMID homologue internal NADH dehydrogenase (NDI1), but not external NADH dehydrogenase (NDE1), can cause apoptosis-like cell death, and this effect can be repressed by increased respiration on glucose-limited media. This result indicates that the regulatory network of energy metabolism, in particular the cross-talk between mitochondria and the rest of the cell, is involved in Ndi1p-induced yeast cell apoptosis. The apoptotic effect of NDI1 overexpression is associated with increased production of reactive oxygen species (ROS) in mitochondria. In addition, NDI1 overexpression in sod2 background causes cell lethality in both fermentable and semifermentable media. Interruption of certain components in the electron transport chain can suppress the growth inhibition from Ndi1p overexpression. We finally show that disruption of NDI1 or NDE1 decreases ROS production and elongates the chronological life span of yeast, accompanied by the loss of survival fitness. Implication of these findings for Ndi1p-induced apoptosis is discussed.

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Akintade, Damilare D., and Bhabatosh Chaudhuri. "Sensing the Generation of Intracellular Free Electrons Using the Inactive Catalytic Subunit of Cytochrome P450s as a Sink." Sensors 20, no. 14 (July 21, 2020): 4050. http://dx.doi.org/10.3390/s20144050.

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Cytochrome P450 reductase (CPR) abstracts electrons from Nicotinamide adenine dinucleotide phosphate H (NADPH), transferring them to an active Cytochrome P450 (CYP) site to provide a functional CYP. In the present study, a yeast strain was genetically engineered to delete the endogenous CPR gene. A human CYP expressed in a CPR-null (yRD−) strain was inactive. It was queried if Bax—which induces apoptosis in yeast and human cells by generating reactive oxygen species (ROS)—substituted for the absence of CPR. Since Bax-generated ROS stems from an initial release of electrons, is it possible for these released electrons to be captured by an inactive CYP to make it active once again? In this study, yeast cells that did not contain any CPR activity (i.e., because the yeasts’ CPR gene was completely deleted) were used to show that (a) human CYPs produced within CPR-null (yRD-) yeast cells were inactive and (b) low levels of the pro-apoptotic human Bax protein could activate inactive human CYPs within this yeast cells. Surprisingly, Bax activated three inactive CYP proteins, confirming that it could compensate for CPR’s absence within yeast cells. These findings could be useful in research, development of bioassays, bioreactors, biosensors, and disease diagnosis, among others.

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Guérin, Renée, Geneviève Arseneault, Stéphane Dumont, and Luis A. Rokeach. "Calnexin Is Involved in Apoptosis Induced by Endoplasmic Reticulum Stress in the Fission Yeast." Molecular Biology of the Cell 19, no. 10 (October 2008): 4404–20. http://dx.doi.org/10.1091/mbc.e08-02-0188.

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Stress conditions affecting the functions of the endoplasmic reticulum (ER) cause the accumulation of unfolded proteins. ER stress is counteracted by the unfolded-protein response (UPR). However, under prolonged stress the UPR initiates a proapoptotic response. Mounting evidence indicate that the ER chaperone calnexin is involved in apoptosis caused by ER stress. Here, we report that overexpression of calnexin in Schizosaccharomyces pombe induces cell death with apoptosis markers. Cell death was partially dependent on the Ire1p ER-stress transducer. Apoptotic death caused by calnexin overexpression required its transmembrane domain (TM), and involved sequences on either side of the ER membrane. Apoptotic death caused by tunicamycin was dramatically reduced in a strain expressing endogenous levels of calnexin lacking its TM and cytosolic tail. This demonstrates the involvement of calnexin in apoptosis triggered by ER stress. A genetic screen identified the S. pombe homologue of the human antiapoptotic protein HMGB1 as a suppressor of apoptotic death due to calnexin overexpression. Remarkably, overexpression of human calnexin in S. pombe also provoked apoptotic death. Our results argue for the conservation of the role of calnexin in apoptosis triggered by ER stress, and validate S. pombe as a model to elucidate the mechanisms of calnexin-mediated cell death.

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Fahrenkrog, Birthe. "Nma111p, the pro-apoptotic HtrA-like nuclear serine protease in Saccharomyces cerevisiae: a short survey." Biochemical Society Transactions 39, no. 5 (September 21, 2011): 1499–501. http://dx.doi.org/10.1042/bst0391499.

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The baker's yeast, Saccharomyces cerevisiae, is also capable of undergoing programmed cell death or apoptosis, for example in response to viral infection as well as during chronological and replicative aging. Intrinsically, programmed cell death in yeast can be induced by, for example, H2O2, acetic acid or the mating-type pheromone. A number of evolutionarily conserved apoptosis-regulatory proteins have been identified in yeast, one of which is the HtrA (high-temperature requirement A)-like serine protease Nma111p (Nma is nuclear mediator of apoptosis). Nma111p is a nuclear serine protease of the HtrA family, which targets Bir1p, the only known inhibitor-of-apoptosis protein in yeast. Nma111p mediates apoptosis in a serine-protease-dependent manner and exhibits its activity exclusively in the nucleus. How the activity of Nma111p is regulated has remained largely elusive, but some evidence points to a control by phosphorylation. Current knowledge of Nma111p's function in apoptosis will be discussed in the present review.

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Mazzoni, Cristina, Eva Herker, Vanessa Palermo, Helmut Jungwirth, Tobias Eisenberg, Frank Madeo, and Claudio Falcone. "Yeast caspase 1 links messenger RNA stability to apoptosis in yeast." EMBO reports 6, no. 11 (September 9, 2005): 1076–81. http://dx.doi.org/10.1038/sj.embor.7400514.

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Cui, Yixian, Shanke Zhao, Zhihao Wu, Pinghua Dai, and Bing Zhou. "Mitochondrial release of the NADH dehydrogenase Ndi1 induces apoptosis in yeast." Molecular Biology of the Cell 23, no. 22 (November 15, 2012): 4373–82. http://dx.doi.org/10.1091/mbc.e12-04-0281.

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Saccharomyces cerevisiae NDI1 codes for the internal mitochondrial ubiquinone oxidoreductase, which transfers electrons from NADH to ubiquinone in the respiratory chain. Previously we found that Ndi1 is a yeast homologue of the protein apoptosis-inducing factor–homologous mitochondrion-associated inducer of death and displays potent proapoptotic activity. Here we show that S. cerevisiae NDI1 is involved in apoptosis induced by various stimuli tested, including H2O2, Mn, and acetate acid, independent of Z-VAD-fmk (a caspase inhibitor) inhibition. Although Ndi1 also participates in respiration, its proapoptotic property is separable from the ubiquinone oxidoreductase activity. During apoptosis, the N-terminal of Ndi1 is cleaved off in the mitochondria, and this activated form then escapes out to execute its apoptotic function. The N-terminal cleavage appears to be essential for the manifestation of the full apoptotic activity, as the uncleaved form of Ndi1 exhibits much less growth-inhibitory activity. Our results thus indicate an important role of Ndi1 in the switch of life and death fates in yeast: during normal growth, Ndi1 assimilates electrons to the electron transport chain and initiates the respiration process to make ATP, whereas under stresses, it cleaves the toxicity-sequestering N-terminal cap, is released from the mitochondria, and becomes a cell killer.

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Fleury, Christophe, Mathieu Pampin, Agathe Tarze, and Bernard Mignotte. "Yeast as a Model to Study Apoptosis?" Bioscience Reports 22, no. 1 (February 1, 2002): 59–79. http://dx.doi.org/10.1023/a:1016013123094.

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Programmed cell death (PCD) serves as a major mechanism for the precise regulation of cell numbers, and as a defense mechanism to remove unwanted and potentially dangerous cells. Despite the striking heterogeneity of cell death induction pathways, the execution of the death program is often associated with characteristic morphological and biochemical changes termed apoptosis. Although for a long time the absence of mitochondrial changes was considered as a hallmark of apoptosis, mitochondria appear today as the central executioner of programmed cell death. This crucial position of mitochondria in programmed cell death control is not due to a simple loss of function (deficit in energy supplying), but rather to an active process in the regulation of effector mechanisms. The large diversity of regulators of apoptosis in mammals and their numerous interactions complicate the analysis of their individual functions. Yeast, eukaryotic but unicellular organism, lack the main regulators of apoptosis (caspases, Bcl-2 family members, …) found in mammals. This absence render them a powerful tool for heterologous expression, functional studies, and even cloning of new regulators of apoptosis. Great advances have thus been made in our understanding of the molecular mechanisms of Bcl-2 family members interactions with themselves and other cellular proteins, specially thanks to the two hybrid system and the easy manipulation of yeast (molecular biology and genetics). This review will focus on the use of yeast as a tool to identify new regulators and study function of mammalian apoptosis regulators.

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Shaham, Shai, Marc A. Shuman, and Ira Herskowitz. "Death-Defying Yeast Identify Novel Apoptosis Genes." Cell 92, no. 4 (February 1998): 425–27. http://dx.doi.org/10.1016/s0092-8674(00)80934-4.

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Matsuyama, Shigemi, Shahrzad Nouraini, and John C. Reed. "Yeast as a tool for apoptosis research." Current Opinion in Microbiology 2, no. 6 (December 1999): 618–23. http://dx.doi.org/10.1016/s1369-5274(99)00031-4.

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LOW, C., L. LIEW, S. PERVAIZ, and H. YANG. "Apoptosis and lipoapoptosis in the fission yeast." FEMS Yeast Research 5, no. 12 (December 2005): 1199–206. http://dx.doi.org/10.1016/j.femsyr.2005.07.004.

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Ink, B., M. Zörnig, B. Baum, N. Hajibagheri, C. James, T. Chittenden, and G. Evan. "Human Bak induces cell death in Schizosaccharomyces pombe with morphological changes similar to those with apoptosis in mammalian cells." Molecular and Cellular Biology 17, no. 5 (May 1997): 2468–74. http://dx.doi.org/10.1128/mcb.17.5.2468.

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Apoptosis as a form of programmed cell death (PCD) in multicellular organisms is a well-established genetically controlled process that leads to elimination of unnecessary or damaged cells. Recently, PCD has also been described for unicellular organisms as a process for the socially advantageous regulation of cell survival. The human Bcl-2 family member Bak induces apoptosis in mammalian cells which is counteracted by the Bcl-x(L) protein. We show that Bak also kills the unicellular fission yeast Schizosaccharomyces pombe and that this is inhibited by coexpression of human Bcl-x(L). Moreover, the same critical BH3 domain of Bak that is required for induction of apoptosis in mammalian cells is also required for inducing death in yeast. This suggests that Bak kills mammalian and yeast cells by similar mechanisms. The phenotype of the Bak-induced death in yeast involves condensation and fragmentation of the chromatin as well as dissolution of the nuclear envelope, all of which are features of mammalian apoptosis. These data suggest that the evolutionarily conserved metazoan PCD pathway is also present in unicellular yeast.

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Polčic, Peter, and Marek Mentel. "Reconstituting the Mammalian Apoptotic Switch in Yeast." Genes 11, no. 2 (January 29, 2020): 145. http://dx.doi.org/10.3390/genes11020145.

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Proteins of the Bcl-2 family regulate the permeabilization of the mitochondrial outer membrane that represents a crucial irreversible step in the process of induction of apoptosis in mammalian cells. The family consists of both proapoptotic proteins that facilitate the membrane permeabilization and antiapoptotic proteins that prevent it in the absence of an apoptotic signal. The molecular mechanisms, by which these proteins interact with each other and with the mitochondrial membranes, however, remain under dispute. Although yeast do not have apparent homologues of these apoptotic regulators, yeast cells expressing mammalian members of the Bcl-2 family have proved to be a valuable model system, in which action of these proteins can be effectively studied. This review focuses on modeling the activity of proapoptotic as well as antiapoptotic proteins of the Bcl-2 family in yeast.

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de Souza, P. M., and M. A. Lindsay. "Mammalian Sterile20-like kinase 1 and the regulation of apoptosis." Biochemical Society Transactions 32, no. 3 (June 1, 2004): 485–88. http://dx.doi.org/10.1042/bst0320485.

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Mammalian Sterile20-like kinase 1 (Mst1) is a ubiquitously expressed serine/threonine kinase which represents a member of the rapidly expanding family of enzymes related to the yeast Sterile20 kinase. Although the physiological function of Mst1 and its role in intracellular signalling is still unclear, reports to date suggest that Mst1, similar to its yeast homologue, operates in the MAPK (mitogen-activated protein kinase) pathway and, in this capacity, may represent a putative MAPK kinase kinase kinase. Moreover, there is abundant evidence for a role of this enzyme in apoptosis, where not only is it a target for caspases, but may also serve as an activator of these proteases to amplify the apoptotic signalling pathway. This paper reviews the investigations that have led to our current understanding of the mechanisms by which Mst1 may be activated and thereby contribute to apoptosis.

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Akintade, Damilare D., and Bhabatosh Chaudhuri. "Apoptosis, Induced by Human α-Synuclein in Yeast, Can Occur Independent of Functional Mitochondria." Cells 9, no. 10 (September 29, 2020): 2203. http://dx.doi.org/10.3390/cells9102203.

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Human α-synuclein expression in baker’s yeast reportedly induces mitochondria-dependent apoptosis. Surprisingly, we find that, under de-repressing conditions of the inducible MET25/GAL1 promoters, yeast cells expressing chromosomally-integrated copies of the human α-synuclein gene are not killed, but spontaneously form respiration-deficient rho-minus (ρ−) petites. Although yeast cells can undergo cell death (apoptosis) from loss of mitochondrial function, they can also survive without functional mitochondria. Such cells are referred to as ρ0 or ρ− petites. This study reports that minimal expression of human α-synuclein in yeast, from MET25/GAL1 promoter, gives rise to ρ− petites. Interestingly, the full expression of α-synuclein, from the same promoters, in α-synuclein-triggered ρ− petites and also in ρ0 petites (produced by treating ρ+ cells with the mutagen ethidium bromide) initiates apoptosis. The percentages of petites increase with increasing α-synuclein gene copy-number. ρ− petites expressing α-synuclein from fully-induced MET25/GAL1 promoters exhibit increased ROS levels, loss of mitochondrial membrane potential, and nuclear DNA fragmentation, with increasing copies of α-synuclein. Our results indicate that, for the first time in yeast, α-synuclein-triggered apoptosis can occur independently of functional mitochondria. The observation that α-synuclein naturally forms petites and that they can undergo apoptosis may have important implications in understanding the pathogenesis of Parkinson’s disease.

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Journal articles on the topic 'Yeast apoptosis'

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