Old yellow enzyme interferes with Bax-induced NADPH loss and lipid peroxidation in yeast

Authors

  • Rieka Reekmans,

    1. Unit of Fundamental and Applied Molecular Biology, Department for Molecular Biomedical Research, VIB-Ghent University, Technologiepark 927, B-9052 Zwijnaarde, Belgium
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  • Kris De Smet,

    1. Unit of Fundamental and Applied Molecular Biology, Department for Molecular Biomedical Research, VIB-Ghent University, Technologiepark 927, B-9052 Zwijnaarde, Belgium
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  • Cuiying Chen,

    1. Unit of Fundamental and Applied Molecular Biology, Department for Molecular Biomedical Research, VIB-Ghent University, Technologiepark 927, B-9052 Zwijnaarde, Belgium
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  • Paul Van Hummelen,

    1. Microarray Facility, Flanders Interuniversity Institute for Biotechnology (VIB), B-3000, Leuven, Belgium
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  • Roland Contreras

    Corresponding author
    1. Unit of Fundamental and Applied Molecular Biology, Department for Molecular Biomedical Research, VIB-Ghent University, Technologiepark 927, B-9052 Zwijnaarde, Belgium
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*Corresponding author. Tel.: +32 9 331 3631; fax: +32 9 331 3502/3609, E-mail address: roland.contreras@dmbr.ugent.be

Abstract

The yeast transcriptional response to murine Bax expression was compared with the changes induced by H2O2 treatment via microarray technology. Although most of the Bax-responsive genes were also triggered by H2O2 treatment, OYE3, ICY2, MLS1 and BTN2 were validated to have a Bax-specific transcriptional response not shared with the oxidative stress trigger. In knockout experiments, only deletion of OYE3, coding for yeast Old yellow enzyme, attenuated the rate of Bax-induced growth arrest, cell death and NADPH decrease. Lipid peroxidation was completely absent in ΔOYE3 expressing Bax. However, the absence of OYE3 sensitized yeast cells to H2O2-induced cell death, and increased the rate of NADPH decrease and lipid peroxidation. Our results clearly indicate that OYE3 interferes with Bax- and H2O2-induced lipid peroxidation and cell death in Saccharomyces cerevisiae.

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