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Identification of a mitochondrial superoxide dismutase with an unusual targeting sequence in Plasmodium falciparum.

By Natasha Sienkiewicz, Wassim Daher, Daniel Dive, Carsten Wrenger, Eric Viscogliosi, René Wintjens, Helène Jouin, Monique Capron, Sylke Müller and Jamal Khalife

Abstract

The intraerythrocytic stages of Plasmodium falciparum are exposed to oxidative stress and require functional anti-oxidant systems to survive. In addition to the parasite's known iron-dependent superoxide dismutase PfSOD1, a second SOD gene (PfSOD2) interrupted by 8 introns was identified on chromosome 6. Molecular modelling shows that the structure of PfSOD2 is similar to other iron-dependent SODs and phylogenetic analysis suggests PfSOD1 and PfSOD2 are the result of an ancestral gene duplication. The deduced amino acid sequence of PfSOD2 is similar to PfSOD1 but has a long N-terminal extension. Immunofluorescence studies show that PfSOD1 is cytosolic, whereas the N-terminal extension of PfSOD2 targets a green fluorescent protein fusion into the parasite's mitochondrion. Both SOD genes are transcribed during the erythrocytic cycle with PfSOD1 mRNA levels up to 35-fold higher than those of PfSOD2. Northern blots demonstrated that the mRNA levels of both SOD genes are up-regulated upon exposure to oxidative stress.Journal ArticleResearch Support, Non-U.S. Gov'tinfo:eu-repo/semantics/publishe

Topics: Biologie, Adaptation, Psychological, Amino Acid Sequence, Animals, Cytoplasm -- enzymology, DNA, Complementary, DNA, Protozoan -- chemistry, Erythrocytes -- parasitology, Fluorescent Antibody Technique, Indirect, Gene Duplication, Gene Expression Regulation, Introns -- genetics, Mitochondria -- enzymology, Models, Molecular, Molecular Sequence Data, Oxidative Stress, Phylogeny, Plasmodium falciparum -- enzymology -- genetics -- growth & development, Protein Sorting Signals, Protein Transport, RNA, Messenger -- analysis, RNA, Protozoan -- analysis, Recombinant Fusion Proteins -- metabolism, Sequence Analysis, DNA, Sequence Homology, Superoxide Dismutase -- chemistry -- genetics -- metabolism, Biologie structurale
Publisher: 'Elsevier BV'
Year: 2004
DOI identifier: 10.1016/j.molbiopara.2004.05.005
OAI identifier: oai:dipot.ulb.ac.be:2013/111233
Provided by: DI-fusion
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