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

Aksam, E. B., Jungwirth, H., Kohlwein, S. D., Ring, J., Madeo, F., Veenhuis, M. & van der Klei, I. J., 15-Oct-2008, In : Free Radical Biology and Medicine. 45, 8, p. 1115-1124 10 p.

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DOI

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

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

Original languageEnglish
Pages (from-to)1115-1124
Number of pages10
JournalFree Radical Biology and Medicine
Volume45
Issue number8
Publication statusPublished - 15-Oct-2008

    Keywords

  • Peroxisome, ROS, Peroxiredoxin, Cell death, YEAST HANSENULA-POLYMORPHA, METHYLOTROPHIC YEAST, METHANOL METABOLISM, CANDIDA-BOIDINII, ALCOHOL OXIDASE, OXIDATIVE STRESS, IMPORT RECEPTOR, MATRIX PROTEIN, GENE ENCODES, MEMBRANE

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