Mitochondrial targeting of peroxiredoxin 5 is preserved from annelids to mammals but is absent in pig Sus scrofa domesticus |
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| Authors: | Valérie Van der Eecken André Clippe Paul P Van Veldhoven Bernard Knoops |
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| Institution: | aUniversité catholique de Louvain, Institut des Sciences de la Vie (ISV), 4–5 place Croix du Sud, B-1348 Louvain-la-Neuve, Belgium;bKatholieke Universiteit Leuven, Department of Molecular Cell Biology, LIPIT, Campus Gasthuisberg, Herestraat, B-3000 Leuven, Belgium |
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| Abstract: | Peroxiredoxin 5 (PRDX5) is a thioredoxin peroxidase able to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. In human, PRDX5 was reported to be localized in the cytosol, the mitochondria, the peroxisomes and the nucleus. Mitochondrial localization results from the presence of an N-terminal mitochondrial targeting sequence (MTS). Here, we examined the conservation of mitochondrial localization of PRDX5 in animal species. We found that PRDX5 MTS is present and functional in the annelid lugworm Arenicola marina. Surprisingly, although mitochondrial targeting is well conserved among animals, PRDX5 is missing in mitochondria of domestic pig. Thus, it appears that mitochondrial targeting of PRDX5 may have been lost throughout evolution in animal species, including pig, with unknown functional consequences. |
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| Keywords: | Abbreviations: AmPRDX5 Arenicola marinaperoxiredoxin 5 DTT dithiothreitol GFP Green Fluorescent Protein GPX glutathione peroxidase HsPRDX5 Homo sapiens peroxiredoxin 5 L-PRDX5 long form of peroxiredoxin 5 MTS mitochondrial targeting sequence PRDX peroxiredoxin RNS reactive nitrogen species ROS reactive oxygen species S-PRDX5 short form of peroxiredoxin 5 SsPRDX5 Sus scrofa peroxiredoxin 5 t-BHP tert-butyl hydroperoxide |
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