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Mitochondrial targeting of peroxiredoxin 5 is preserved from annelids to mammals but is absent in pig Sus scrofa domesticus.

Authors :
UCL - SST/ISV - Institut des sciences de la vie
Katholieke Universiteit Leuven - Department of Molecular Cell Biology, LIPIT, Leuven, Belgium
Van der Eecken, Valérie
Clippe, André
Van Veldhoven, Paul P
Knoops, Bernard
UCL - SST/ISV - Institut des sciences de la vie
Katholieke Universiteit Leuven - Department of Molecular Cell Biology, LIPIT, Leuven, Belgium
Van der Eecken, Valérie
Clippe, André
Van Veldhoven, Paul P
Knoops, Bernard
Source :
Mitochondrion, Vol. 11, no. 6, p. 973-81 (2011)
Publication Year :
2011

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.

Details

Database :
OAIster
Journal :
Mitochondrion, Vol. 11, no. 6, p. 973-81 (2011)
Notes :
English
Publication Type :
Electronic Resource
Accession number :
edsoai.on1130524789
Document Type :
Electronic Resource