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1. Discourse-Directed Framing as Communication Strategy Alters Students' Concept of Antibiotics and Antibiotic Resistance Formation

Author

Beranek-Knauer, Heide, Walter, Hildrun, Paleczek, Dominik, Eder, Lucas, Jungwirth, Kerstin, and Jungwirth, Helmut

Abstract

One of the most urgent matters in current medicine is the preservation of antibiotic treatment options due to an increasing threat of antibiotic resistance in pathogenic microorganisms. Therefore, increasing awareness by adapted science education and communication regarding this topic is of the utmost importance. This article shows that an out-of-school laboratory course using active learning techniques is a valuable contribution to traditional teaching inciting personal and social responsibility. Attitude toward science (BRAINS), value of science to society (MATS), situational interest and emotions were tested. The participants' conception of antibiotics was evaluated by analysing follow-up mind maps. Generally, the laboratory course created positive feelings and situational interest. Compared to an instructor-directed frame, communication within an individually adapting discourse-directed frame conveyed more wide-spread perception of the topic, including societal and personal implications. The outcome of the study provides evidence that an out-of-school laboratory course can be a valuable tool for interest development in socio-scientific issues. Discourse-directed framing, in this environment, improves the individual ability to alter social and personal responsibility regarding science topics.

Published
2020
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2. Chronological Aging Leads to Apoptosis in Yeast

Author

Herker, Eva, Jungwirth, Helmut, Lehmann, Katharina A., Maldener, Corinna, Fröhlich, Kai-Uwe, Wissing, Silke, Büttner, Sabrina, Fehr, Markus, Sigrist, Stephan, and Madeo, Frank

Published
2004

8. Guidelines and recommendations on yeast cell death nomenclature

Author

Carmona-Gutierrez, Didac, Bauer, Maria Anna, Zimmermann, Andreas, Aguilera, Andres, Austriaco, Nicanor, Ayscough, Kathryn, Balzan, Rena, Bar-Nun, Shoshana, Barrientos, Antonio, Belenky, Peter, Blondel, Marc, Braun, Ralf J., Breitenbach, Michael, Burhans, William C., Büttner, Sabrina, Cavalieri, Duccio, Chang, Michael, Cooper, Katrina F., Corte-Real, Manuela, Costa, Vitor, Cullin, Christophe, Dawes, Ian, Dengjel, Jorn, Dickman, Martin B., Eisenberg, Tobias, Fahrenkrog, Birthe, Fasel, Nicolas, Frohlich, Kai-Uwe, Gargouri, Ali, Giannattasio, Sergio, Goffrini, Paola, Gourlay, Campbell W., Grant, Chris M., Greenwood, Michael T., Guaragnella, Nicoletta, Heger, Thomas, Heinisch, Juergen, Herker, Eva, Herrmann, Johannes M., Hofer, Sebastian, Jimenez-Ruiz, Antonio, Jungwirth, Helmut, Kainz, Katharina, Kontoyiannis, Dimitrios P., Ludovico, Paula, Manon, Stephen, Martegani, Enzo, Mazzoni, Cristina, Megeney, Lynn A., Meisinger, Chris, Nielsen, Jens, Nystrom, Thomas, Osiewacz, Heinz D., Outeiro, Tiago F., Park, Hay-Oak, Pendl, Tobias, Petranovic, Dina, Picot, Stephane, Polcic, Peter, Powers, Ted, Ramsdale, Mark, Rinnerthaler, Mark, Rockenfeller, Patrick, Ruckenstuhl, Christoph, Schaffrath, Raffael, Segovia, Maria, Severin, Fedor F., Sharon, Amir, Sigrist, Stephan J., Sommer-Ruck, Cornelia, Sousa, Maria Joao, Thevelein, Johan M., Thevissen, Karin, Titorenko, Vladimir, Toledano, Michel B., Tuite, Mick, Voegtle, F. -Nora, Westermann, Benedikt, Winderickx, Joris, Wissing, Silke, Woelfl, Stefan, Zhang, Zhaojie J., Zhao, Richard Y., Zhou, Bing, Galluzzi, Lorenzo, Kroemer, Guido, Madeo, Frank, Carmona-Gutierrez, Didac, Bauer, Maria Anna, Zimmermann, Andreas, Aguilera, Andres, Austriaco, Nicanor, Ayscough, Kathryn, Balzan, Rena, Bar-Nun, Shoshana, Barrientos, Antonio, Belenky, Peter, Blondel, Marc, Braun, Ralf J., Breitenbach, Michael, Burhans, William C., Büttner, Sabrina, Cavalieri, Duccio, Chang, Michael, Cooper, Katrina F., Corte-Real, Manuela, Costa, Vitor, Cullin, Christophe, Dawes, Ian, Dengjel, Jorn, Dickman, Martin B., Eisenberg, Tobias, Fahrenkrog, Birthe, Fasel, Nicolas, Frohlich, Kai-Uwe, Gargouri, Ali, Giannattasio, Sergio, Goffrini, Paola, Gourlay, Campbell W., Grant, Chris M., Greenwood, Michael T., Guaragnella, Nicoletta, Heger, Thomas, Heinisch, Juergen, Herker, Eva, Herrmann, Johannes M., Hofer, Sebastian, Jimenez-Ruiz, Antonio, Jungwirth, Helmut, Kainz, Katharina, Kontoyiannis, Dimitrios P., Ludovico, Paula, Manon, Stephen, Martegani, Enzo, Mazzoni, Cristina, Megeney, Lynn A., Meisinger, Chris, Nielsen, Jens, Nystrom, Thomas, Osiewacz, Heinz D., Outeiro, Tiago F., Park, Hay-Oak, Pendl, Tobias, Petranovic, Dina, Picot, Stephane, Polcic, Peter, Powers, Ted, Ramsdale, Mark, Rinnerthaler, Mark, Rockenfeller, Patrick, Ruckenstuhl, Christoph, Schaffrath, Raffael, Segovia, Maria, Severin, Fedor F., Sharon, Amir, Sigrist, Stephan J., Sommer-Ruck, Cornelia, Sousa, Maria Joao, Thevelein, Johan M., Thevissen, Karin, Titorenko, Vladimir, Toledano, Michel B., Tuite, Mick, Voegtle, F. -Nora, Westermann, Benedikt, Winderickx, Joris, Wissing, Silke, Woelfl, Stefan, Zhang, Zhaojie J., Zhao, Richard Y., Zhou, Bing, Galluzzi, Lorenzo, Kroemer, Guido, and Madeo, Frank

Abstract

Elucidating the biology of yeast in its full complexity has major implications for science, medicine and industry. One of the most critical processes determining yeast life and physiology is cellular demise. However, the investigation of yeast cell death is a relatively young field, and a widely accepted set of concepts and terms is still missing. Here, we propose unified criteria for the definition of accidental, regulated, and programmed forms of cell death in yeast based on a series of morphological and biochemical criteria. Specifically, we provide consensus guidelines on the differential definition of terms including apoptosis, regulated necrosis, and autophagic cell death, as we refer to additional cell death routines that are relevant for the biology of (at least some species of) yeast. As this area of investigation advances rapidly, changes and extensions to this set of recommendations will be implemented in the years to come. Nonetheless, we strongly encourage the authors, reviewers and editors of scientific articles to adopt these collective standards in order to establish an accurate framework for yeast cell death research and, ultimately, to accelerate the progress of this vibrant field of research.

Published
2018
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9. Guidelines and recommendations on yeast cell death nomenclature

Author

Carmona-Gutierrez, D, Bauer, M, Zimmermann, A, Aguilera, A, Austriaco, N, Ayscough, K, Balzan, R, Bar-Nun, S, Barrientos, A, Belenky, P, Blondel, M, Braun, R, Breitenbach, M, Burhans, W, Buettner, S, Cavalieri, D, Chang, M, Cooper, K, Côrte-Real, M, Costa, V, Cullin, C, Dawes, I, Dengjel, J, Dickman, M, Eisenberg, T, Fahrenkrog, B, Fasel, N, Froehlich, K, Gargouri, A, Giannattasio, S, Goffrini, P, Gourlay, C, Grant, C, Greenwood, M, Guaragnella, N, Heger, T, Heinisch, J, Herker, E, Herrmann, J, Hofer, S, Jiménez-Ruiz, A, Jungwirth, H, Kainz, K, Kontoyiannis, D, Ludovico, P, Manon, S, Martegani, E, Mazzoni, C, Megeney, L, Meisinger, C, Nielsen, J, Nystroem, T, Osiewacz, H, Outeiro, T, Park, H, Pendl, T, Petranovic, D, Picot, S, Polčic, P, Powers, T, Ramsdale, M, Rinnerthaler, M, Rockenfeller, P, Ruckenstuhl, C, Schaffrath, R, Segovia, M, Severin, F, Sharon, A, Sigrist, S, Sommer-Ruck, C, Sousa, M, Thevelein, J, Thevissen, K, Titorenko, V, Toledano, M, Tuite, M, Voegtle, F, Westermann, B, Winderickx, J, Wissing, S, Woelfl, S, Zhang, Z, Zhao, R, Zhou, B, Galluzzi, L, Kroemer, G, Madeo, F, Carmona-Gutierrez, Didac, Bauer, Maria Anna, Zimmermann, Andreas, Aguilera, Andrés, Austriaco, Nicanor, Ayscough, Kathryn, Balzan, Rena, Bar-Nun, Shoshana, Barrientos, Antonio, Belenky, Peter, Blondel, Marc, Braun, Ralf J., Breitenbach, Michael, Burhans, William C., Buettner, Sabrina, Cavalieri, Duccio, Chang, Michael, Cooper, Katrina F., Côrte-Real, Manuela, Costa, Vítor, Cullin, Christophe, Dawes, Ian, Dengjel, Jörn, Dickman, Martin B., Eisenberg, Tobias, Fahrenkrog, Birthe, Fasel, Nicolas, Froehlich, Kai-Uwe, Gargouri, Ali, Giannattasio, Sergio, Goffrini, Paola, Gourlay, Campbell W., Grant, Chris M., Greenwood, Michael T., Guaragnella, Nicoletta, Heger, Thomas, Heinisch, Juergen, Herker, Eva, Herrmann, Johannes M., Hofer, Sebastian, Jiménez-Ruiz, Antonio, Jungwirth, Helmut, Kainz, Katharina, Kontoyiannis, Dimitrios P., Ludovico, Paula, Manon, Stéphen, Martegani, Enzo, Mazzoni, Cristina, Megeney, Lynn A., Meisinger, Chris, Nielsen, Jens, Nystroem, Thomas, Osiewacz, Heinz D., Outeiro, Tiago F., Park, Hay-Oak, Pendl, Tobias, Petranovic, Dina, Picot, Stephane, Polčic, Peter, Powers, Ted, Ramsdale, Mark, Rinnerthaler, Mark, Rockenfeller, Patrick, Ruckenstuhl, Christoph, Schaffrath, Raffael, Segovia, Maria, Severin, Fedor F., Sharon, Amir, Sigrist, Stephan J., Sommer-Ruck, Cornelia, Sousa, Maria João, Thevelein, Johan M., Thevissen, Karin, Titorenko, Vladimir, Toledano, Michel B., Tuite, Mick, Voegtle, F. -Nora, Westermann, Benedikt, Winderickx, Joris, Wissing, Silke, Woelfl, Stefan, Zhang, Zhaojie J., Zhao, Richard Y., Zhou, Bing, Galluzzi, Lorenzo, Kroemer, Guido, Madeo, Frank, Carmona-Gutierrez, D, Bauer, M, Zimmermann, A, Aguilera, A, Austriaco, N, Ayscough, K, Balzan, R, Bar-Nun, S, Barrientos, A, Belenky, P, Blondel, M, Braun, R, Breitenbach, M, Burhans, W, Buettner, S, Cavalieri, D, Chang, M, Cooper, K, Côrte-Real, M, Costa, V, Cullin, C, Dawes, I, Dengjel, J, Dickman, M, Eisenberg, T, Fahrenkrog, B, Fasel, N, Froehlich, K, Gargouri, A, Giannattasio, S, Goffrini, P, Gourlay, C, Grant, C, Greenwood, M, Guaragnella, N, Heger, T, Heinisch, J, Herker, E, Herrmann, J, Hofer, S, Jiménez-Ruiz, A, Jungwirth, H, Kainz, K, Kontoyiannis, D, Ludovico, P, Manon, S, Martegani, E, Mazzoni, C, Megeney, L, Meisinger, C, Nielsen, J, Nystroem, T, Osiewacz, H, Outeiro, T, Park, H, Pendl, T, Petranovic, D, Picot, S, Polčic, P, Powers, T, Ramsdale, M, Rinnerthaler, M, Rockenfeller, P, Ruckenstuhl, C, Schaffrath, R, Segovia, M, Severin, F, Sharon, A, Sigrist, S, Sommer-Ruck, C, Sousa, M, Thevelein, J, Thevissen, K, Titorenko, V, Toledano, M, Tuite, M, Voegtle, F, Westermann, B, Winderickx, J, Wissing, S, Woelfl, S, Zhang, Z, Zhao, R, Zhou, B, Galluzzi, L, Kroemer, G, Madeo, F, Carmona-Gutierrez, Didac, Bauer, Maria Anna, Zimmermann, Andreas, Aguilera, Andrés, Austriaco, Nicanor, Ayscough, Kathryn, Balzan, Rena, Bar-Nun, Shoshana, Barrientos, Antonio, Belenky, Peter, Blondel, Marc, Braun, Ralf J., Breitenbach, Michael, Burhans, William C., Buettner, Sabrina, Cavalieri, Duccio, Chang, Michael, Cooper, Katrina F., Côrte-Real, Manuela, Costa, Vítor, Cullin, Christophe, Dawes, Ian, Dengjel, Jörn, Dickman, Martin B., Eisenberg, Tobias, Fahrenkrog, Birthe, Fasel, Nicolas, Froehlich, Kai-Uwe, Gargouri, Ali, Giannattasio, Sergio, Goffrini, Paola, Gourlay, Campbell W., Grant, Chris M., Greenwood, Michael T., Guaragnella, Nicoletta, Heger, Thomas, Heinisch, Juergen, Herker, Eva, Herrmann, Johannes M., Hofer, Sebastian, Jiménez-Ruiz, Antonio, Jungwirth, Helmut, Kainz, Katharina, Kontoyiannis, Dimitrios P., Ludovico, Paula, Manon, Stéphen, Martegani, Enzo, Mazzoni, Cristina, Megeney, Lynn A., Meisinger, Chris, Nielsen, Jens, Nystroem, Thomas, Osiewacz, Heinz D., Outeiro, Tiago F., Park, Hay-Oak, Pendl, Tobias, Petranovic, Dina, Picot, Stephane, Polčic, Peter, Powers, Ted, Ramsdale, Mark, Rinnerthaler, Mark, Rockenfeller, Patrick, Ruckenstuhl, Christoph, Schaffrath, Raffael, Segovia, Maria, Severin, Fedor F., Sharon, Amir, Sigrist, Stephan J., Sommer-Ruck, Cornelia, Sousa, Maria João, Thevelein, Johan M., Thevissen, Karin, Titorenko, Vladimir, Toledano, Michel B., Tuite, Mick, Voegtle, F. -Nora, Westermann, Benedikt, Winderickx, Joris, Wissing, Silke, Woelfl, Stefan, Zhang, Zhaojie J., Zhao, Richard Y., Zhou, Bing, Galluzzi, Lorenzo, Kroemer, Guido, and Madeo, Frank

Abstract

Elucidating the biology of yeast in its full complexity has major implications for science, medicine and industry. One of the most critical processes determining yeast life and physiology is cellular demise. However, the investigation of yeast cell death is a relatively young field, and a widely accepted set of concepts and terms is still missing. Here, we propose unified criteria for the definition of accidental, regulated, and programmed forms of cell death in yeast based on a series of morphological and biochemical criteria. Specifically, we provide consensus guidelines on the differential definition of terms including apoptosis, regulated necrosis, and autophagic cell death, as we refer to additional cell death routines that are relevant for the biology of (at least some species of) yeast. As this area of investigation advances rapidly, changes and extensions to this set of recommendations will be implemented in the years to come. Nonetheless, we strongly encourage the authors, reviewers and editors of scientific articles to adopt these collective standards in order to establish an accurate framework for yeast cell death research and, ultimately, to accelerate the progress of this vibrant field of research.

Published
2018

10. Guidelines and recommendations on yeast cell death nomenclature

Author

Carmona-Gutierrez, Didac, primary, Bauer, Maria Anna, additional, Zimmermann, Andreas, additional, Aguilera, Andrés, additional, Austriaco, Nicanor, additional, Ayscough, Kathryn, additional, Balzan, Rena, additional, Bar-Nun, Shoshana, additional, Barrientos, Antonio, additional, Belenky, Peter, additional, Blondel, Marc, additional, Braun, Ralf J., additional, Breitenbach, Michael, additional, Burhans, William C., additional, Buettner, Sabrina, additional, Cavalieri, Duccio, additional, Chang, Michael, additional, Cooper, Katrina F., additional, Côrte-Real, Manuela, additional, Costa, Vítor, additional, Cullin, Christophe, additional, Dawes, Ian, additional, Dengjel, Jörn, additional, Dickman, Martin B., additional, Eisenberg, Tobias, additional, Fahrenkrog, Birthe, additional, Fasel, Nicolas, additional, Froehlich, Kai-Uwe, additional, Gargouri, Ali, additional, Giannattasio, Sergio, additional, Goffrini, Paola, additional, Gourlay, Campbell W., additional, Grant, Chris M., additional, Greenwood, Michael T., additional, Guaragnella, Nicoletta, additional, Heger, Thomas, additional, Heinisch, Juergen, additional, Herker, Eva, additional, Herrmann, Johannes M., additional, Hofer, Sebastian, additional, Jiménez-Ruiz, Antonio, additional, Jungwirth, Helmut, additional, Kainz, Katharina, additional, Kontoyiannis, Dimitrios P., additional, Ludovico, Paula, additional, Manon, Stéphen, additional, Martegani, Enzo, additional, Mazzoni, Cristina, additional, Megeney, Lynn A., additional, Meisinger, Chris, additional, Nielsen, Jens, additional, Nystroem, Thomas, additional, Osiewacz, Heinz D., additional, Outeiro, Tiago F., additional, Park, Hay-Oak, additional, Pendl, Tobias, additional, Petranovic, Dina, additional, Picot, Stephane, additional, Polčic, Peter, additional, Powers, Ted, additional, Ramsdale, Mark, additional, Rinnerthaler, Mark, additional, Rockenfeller, Patrick, additional, Ruckenstuhl, Christoph, additional, Schaffrath, Raffael, additional, Segovia, Maria, additional, Severin, Fedor F., additional, Sharon, Amir, additional, Sigrist, Stephan J., additional, Sommer-Ruck, Cornelia, additional, Sousa, Maria João, additional, Thevelein, Johan M., additional, Thevissen, Karin, additional, Titorenko, Vladimir, additional, Toledano, Michel B., additional, Tuite, Mick, additional, Voegtle, F.-Nora, additional, Westermann, Benedikt, additional, Winderickx, Joris, additional, Wissing, Silke, additional, Woelfl, Stefan, additional, Zhang, Zhaojie J., additional, Zhao, Richard Y., additional, Zhou, Bing, additional, Galluzzi, Lorenzo, additional, Kroemer, Guido, additional, and Madeo, Frank, additional

Published
2018
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11. Spermidine promotes mating and fertilization efficiency in model organisms

Author

Bauer, Maria Anna, Carmona-Gutiérrez, Didac, Ruckenstuhl, Christoph, Reisenbichler, Angela, Megalou, Evgenia V., Eisenberg, Tobias, Magnes, Christoph, Jungwirth, Helmut, Sinner, Frank M., Pieber, Thomas R., Fröhlich, Kai-Uwe, Kroemer, Guido, Tavernarakis, Nektarios, and Madeo, Frank

Subjects
autophagy, sexual reproduction, fertilization, Spermidine, Report, Animals, Cell Surface Extensions, Saccharomyces cerevisiae, Caenorhabditis elegans, shmoo, Pheromones, mating
Abstract

Spermidine is a naturally occurring polyamine involved in multiple biological processes, including DNA metabolism, autophagy and aging. Like other polyamines, spermidine is also indispensable for successful reproduction at several stages. However, a direct influence on the actual fertilization process, i.e., the fusion of an oocyte with a spermatocyte, remains uncertain. To explore this possibility, we established the mating process in the yeast Saccharomyces cerevisiae as a model for fertilization in higher eukaryotes. During human fertilization, the sperm capacitates and the acrosome reaction is necessary for penetration of the oocyte. Similarly, sexually active yeasts form a protrusion called “shmoo” as a prerequisite for mating. In this study, we demonstrate that pheromone-induced shmoo formation requires spermidine. In addition, we show that spermidine is essential for mating in yeast as well as for egg fertilization in the nematode Caenorhabditis elegans. In both cases, this occurs independently from autophagy. In synthesis, we identify spermidine as an important mating component in unicellular and multicellular model organisms, supporting an unprecedented evolutionary conservation of the mechanisms governing fertilization-related cellular fusion.

Published
2013

12. Systematic Phenotyping of a Large-Scale Candida glabrata Deletion Collection Reveals Novel Antifungal Tolerance Genes

Author

Schwarzmüller, Tobias, primary, Ma, Biao, additional, Hiller, Ekkehard, additional, Istel, Fabian, additional, Tscherner, Michael, additional, Brunke, Sascha, additional, Ames, Lauren, additional, Firon, Arnaud, additional, Green, Brian, additional, Cabral, Vitor, additional, Marcet-Houben, Marina, additional, Jacobsen, Ilse D., additional, Quintin, Jessica, additional, Seider, Katja, additional, Frohner, Ingrid, additional, Glaser, Walter, additional, Jungwirth, Helmut, additional, Bachellier-Bassi, Sophie, additional, Chauvel, Murielle, additional, Zeidler, Ute, additional, Ferrandon, Dominique, additional, Gabaldón, Toni, additional, Hube, Bernhard, additional, d'Enfert, Christophe, additional, Rupp, Steffen, additional, Cormack, Brendan, additional, Haynes, Ken, additional, and Kuchler, Karl, additional

Published
2014
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13. Resveratrol induces antioxidant defence via transcription factor Yap1p

Author

Bioquímica i Biotecnologia, Medicina i Cirurgia, Universitat Rovira i Virgili, Vendrell, Joan, Clotet, Josep, Tinahones, Francisco, Mas, Albert, Cordero, Ricardo R., Madeo, Frank, Jungwirth, Helmut, Carmona-Gutierrez, Didac, Rodriguez-Porrata, Boris, Menoyo, Sandra, Miranda, Merce, Escote, Xavier, Bioquímica i Biotecnologia, Medicina i Cirurgia, Universitat Rovira i Virgili, Vendrell, Joan, Clotet, Josep, Tinahones, Francisco, Mas, Albert, Cordero, Ricardo R., Madeo, Frank, Jungwirth, Helmut, Carmona-Gutierrez, Didac, Rodriguez-Porrata, Boris, Menoyo, Sandra, Miranda, Merce, and Escote, Xavier

Abstract

Resveratrol is a polyphenol suggested to play a protective role against ageing and age-related diseases. We demonstrate that administering low-doses of resveratrol causes ROS accumulation and transcriptional changes in yeast cells and human adipocytes. These changes in gene expression depend on the oxidative transcription factor Yap1p. In particular, resveratrol induces expression of Yap1p gene targets, such as TRX2, TRR1 or AHP1, in a Yap1p-dependent mode. Under resveratrol treatment, Yap1p is phosphorylated and accumulated in the nucleus. Yap1p knockout causes resveratrol sensitivity, which totally depends on the presence of the C-terminal region of Yap1p. Thus, resveratrol may enhance cellular lifespan by hormetic ROS accumulation, which leads to strengthening the cells' antioxidant capacity.Copyright © 2012 John Wiley & Sons, Ltd.

Published
2012

14. Absence of the peroxiredoxin Pmp20 causes peroxisomal protein leakage and necrotic cell death

Author

Aksam, Eda Bener, Jungwirth, Helmut, Kohlwein, Sepp D., Ring, Julia, Madeo, Frank, Veenhuis, Marten, van der Klei, Ida J., Aksam, Eda Bener, Jungwirth, Helmut, Kohlwein, Sepp D., Ring, Julia, Madeo, Frank, Veenhuis, Marten, and van der Klei, Ida J.

Abstract

We analyzed the role of the peroxisomal peroxiredoxin Pmp20 of the yeast Hansenula polymorpha. Cells of a PMP20 disruption strain (pmp20) grew normally on substrates that are not metabolized by peroxisomal enzymes, but showed a severe growth defect on methanol, the metabolism of which involves a hydrogen peroxide producing peroxisomal oxidase. This growth defect was paralleled by leakage of peroxisomal matrix proteins into the cytosol. Methanol-induced pmp20 cells accumulated enhanced levels of reactive oxygen species and lipid peroxidation products. Moreover, the fatty acid composition of methanol-induced pmp20 cells differed relative to WT controls, suggesting an effect on fatty acid homeostasis. Plating assays and FACS-based analysis of cell death markers revealed that pmp20 cells show loss of clonogenic efficiency and membrane integrity, when cultured on methanol. We conclude that the absence of the peroxisomal peroxiredoxin leads to loss of peroxisome membrane integrity and necrotic cell death. (C) 2008 Elsevier Inc. All Fights reserved

Published
2008

16. Resveratrol induces antioxidant defence via transcription factor Yap1p

Author

Escoté, Xavier, primary, Miranda, Merce, additional, Menoyo, Sandra, additional, Rodríguez-Porrata, Boris, additional, Carmona-Gutiérrez, Didac, additional, Jungwirth, Helmut, additional, Madeo, Frank, additional, Cordero, Ricardo R., additional, Mas, Albert, additional, Tinahones, Francisco, additional, Clotet, Josep, additional, and Vendrell, Joan, additional

Published
2012
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21. Functional Mitochondria Are Required for α-Synuclein Toxicity in Aging Yeast

Author

Büttner, Sabrina, primary, Bitto, Alessandro, additional, Ring, Julia, additional, Augsten, Manuela, additional, Zabrocki, Piotr, additional, Eisenberg, Tobias, additional, Jungwirth, Helmut, additional, Hutter, Sylvia, additional, Carmona-Gutierrez, Didac, additional, Kroemer, Guido, additional, Winderickx, Joris, additional, and Madeo, Frank, additional

Published
2008
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23. Apoptosis in yeast

Author

Madeo, Frank, primary, Herker, Eva, additional, Wissing, Silke, additional, Jungwirth, Helmut, additional, Eisenberg, Tobias, additional, and Fröhlich, Kai-Uwe, additional

Published
2004
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26. Systematic Phenotyping of a Large-Scale Candida glabrata Deletion Collection Reveals Novel Antifungal Tolerance Genes.

Author

Schwarzmüller, Tobias, Ma, Biao, Hiller, Ekkehard, Istel, Fabian, Tscherner, Michael, Brunke, Sascha, Ames, Lauren, Firon, Arnaud, Green, Brian, Cabral, Vitor, Marcet-Houben, Marina, Jacobsen, Ilse D., Quintin, Jessica, Seider, Katja, Frohner, Ingrid, Glaser, Walter, Jungwirth, Helmut, Bachellier-Bassi, Sophie, Chauvel, Murielle, and Zeidler, Ute

Subjects
PATHOGENIC microorganisms, FUNGAL genes, CANDIDIASIS, AZOLES, ANTIFUNGAL agents, ECHINOCANDINS, THERAPEUTICS
Abstract

The opportunistic fungal pathogen Candida glabrata is a frequent cause of candidiasis, causing infections ranging from superficial to life-threatening disseminated disease. The inherent tolerance of C. glabrata to azole drugs makes this pathogen a serious clinical threat. To identify novel genes implicated in antifungal drug tolerance, we have constructed a large-scale C. glabrata deletion library consisting of 619 unique, individually bar-coded mutant strains, each lacking one specific gene, all together representing almost 12% of the genome. Functional analysis of this library in a series of phenotypic and fitness assays identified numerous genes required for growth of C. glabrata under normal or specific stress conditions, as well as a number of novel genes involved in tolerance to clinically important antifungal drugs such as azoles and echinocandins. We identified 38 deletion strains displaying strongly increased susceptibility to caspofungin, 28 of which encoding proteins that have not previously been linked to echinocandin tolerance. Our results demonstrate the potential of the C. glabrata mutant collection as a valuable resource in functional genomics studies of this important fungal pathogen of humans, and to facilitate the identification of putative novel antifungal drug target and virulence genes. [ABSTRACT FROM AUTHOR]

Published
2014
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29. Diazaborine Resistance in the Yeast Saccharomyces cerevisiaeReveals a Link between YAP1and the Pleiotropic Drug Resistance Genes PDR1andPDR3*

Author

Wendler, Franz, Bergler, Helmut, Prutej, Katja, Jungwirth, Helmut, Zisser, Gertrude, Kuchler, Karl, and Högenauer, Gregor

Abstract

We have investigated the mechanisms underlying resistance to the drug diazaborine in Saccharomyces cerevisiae. We used UV mutagenesis to generate resistant mutants, which were divided into three different complementation groups. The resistant phenotype in these groups was found to be caused by allelic forms of the genes AFG2, PDR1, andPDR3. The AFG2gene encodes an AAA (ATPases associated to a variety of cellularactivities) protein of unknown function, whilePDR1and PDR3encode two transcriptional regulatory proteins involved in pleiotropic drug resistance development. The isolated PDR1–12and PDR3–33alleles carry mutations that lead to a L1044Q and a Y276H exchange, respectively. In addition, we report that overexpression of Yap1p, the yeast homologue of the transcription factor AP1, results in a diazaborine-resistant phenotype. The YAP1-mediated diazaborine resistance is dependent on the presence of functionalPDR1and PDR3genes, although PDR3had a more pronounced effect. These results provide the first evidence for a functional link between the Yap1p-dependent stress response pathway and Pdr1p/Pdr3p-dependent development of pleiotropic drug resistance.

Published
1997
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30. Functional mitochondria are required for alpha-synuclein toxicity in aging yeast.

Author

Büttner S, Bitto A, Ring J, Augsten M, Zabrocki P, Eisenberg T, Jungwirth H, Hutter S, Carmona-Gutierrez D, Kroemer G, Winderickx J, and Madeo F

Subjects
Caspases metabolism, High-Temperature Requirement A Serine Peptidase 2, Mitochondrial Proteins metabolism, NADH, NADPH Oxidoreductases metabolism, Reactive Oxygen Species, Saccharomyces cerevisiae Proteins metabolism, Serine Endopeptidases metabolism, Apoptosis physiology, Cellular Senescence physiology, Mitochondria metabolism, Models, Biological, Saccharomyces cerevisiae physiology, alpha-Synuclein metabolism
Abstract

alpha-Synuclein is one of the principal toxic triggers of Parkinson disease, an age-associated neurodegeneration. Using old yeast as a model of alpha-synuclein expression in post-mitotic cells, we show that alpha-synuclein toxicity depends on chronological aging and results in apoptosis as well as necrosis. Neither disruption of key components of the unfolded protein response nor deletion of proapoptotic key players (including the yeast caspase YCA1, the apoptosis-inducing factor AIF1, or the serine protease OMI) did prevent alpha-synuclein-induced cell killing. However, abrogation of mitochondrial DNA (rho(0)) inhibited alpha-synuclein-induced reactive oxygen species formation and subsequent apoptotic cell death. Thus, introducing an aging yeast model of alpha-synuclein toxicity, we demonstrate a strict requirement of functional mitochondria.

Published
2008
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