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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2004-7-28
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/superoxide dismutase 1,
http://linkedlifedata.com/resource/pubmed/chemical/superoxide dismutase 2
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0166-6851
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
137
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
121-32
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15279958-Adaptation, Psychological,
pubmed-meshheading:15279958-Amino Acid Sequence,
pubmed-meshheading:15279958-Animals,
pubmed-meshheading:15279958-Cytoplasm,
pubmed-meshheading:15279958-DNA, Complementary,
pubmed-meshheading:15279958-DNA, Protozoan,
pubmed-meshheading:15279958-Erythrocytes,
pubmed-meshheading:15279958-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:15279958-Gene Duplication,
pubmed-meshheading:15279958-Gene Expression Regulation,
pubmed-meshheading:15279958-Introns,
pubmed-meshheading:15279958-Mitochondria,
pubmed-meshheading:15279958-Models, Molecular,
pubmed-meshheading:15279958-Molecular Sequence Data,
pubmed-meshheading:15279958-Oxidative Stress,
pubmed-meshheading:15279958-Phylogeny,
pubmed-meshheading:15279958-Plasmodium falciparum,
pubmed-meshheading:15279958-Protein Sorting Signals,
pubmed-meshheading:15279958-Protein Transport,
pubmed-meshheading:15279958-RNA, Messenger,
pubmed-meshheading:15279958-RNA, Protozoan,
pubmed-meshheading:15279958-Recombinant Fusion Proteins,
pubmed-meshheading:15279958-Sequence Analysis, DNA,
pubmed-meshheading:15279958-Sequence Homology,
pubmed-meshheading:15279958-Superoxide Dismutase
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pubmed:year |
2004
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pubmed:articleTitle |
Identification of a mitochondrial superoxide dismutase with an unusual targeting sequence in Plasmodium falciparum.
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pubmed:affiliation |
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, WTB/MSI Complex, DD15EH, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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