Molecular characterization of the glutathione peroxidase gene of the human malaria parasite Plasmodium falciparum

In this paper we report the isolation and the characterization of a gene encoding the antioxidant enzyme glutathione peroxidase from the human malaria parasite Plasmodium falciparum. This gene contains two introns of 208 and 168 bp and is present in a single copy on chromosome 13. The open reading f...

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Bibliographic Details
Published in:	Molecular and biochemical parasitology Vol. 78; no. 1-2; pp. 237 - 248
Main Authors:	Gamain, Benoît, Langsley, Gordon, Fourmaux, Marie N., Touzel, Jean P., Camus, Daniel, Dive, Daniel, Slomianny, Christian
Format:	Journal Article
Language:	English
Published:	Netherlands Elsevier B.V 01-06-1996 Elsevier
Subjects:	Amino Acid Sequence Animals Base Sequence Binding Sites - genetics Chemical and Process Engineering DNA, Protozoan - genetics Engineering Sciences Food engineering Gene Genes, Protozoan Glutathione peroxidase Glutathione Peroxidase - chemistry Glutathione Peroxidase - genetics Glutathione Peroxidase - metabolism Humans Introns Life Sciences Malaria Molecular Sequence Data Molecular Structure Molecular Weight Nucleic Acid Conformation Phylogenetic tree Phylogeny Plasmodium falciparum Plasmodium falciparum - enzymology Plasmodium falciparum - genetics Polymerase Chain Reaction RNA, Protozoan - chemistry RNA, Protozoan - genetics Selenium Sequence Homology, Amino Acid Sequence Homology, Nucleic Acid Species Specificity Glutathione peroxidase PhGPx Plasmodium falciparum Malaria Gene Phylogenetic tree ROS SOD Selenium GPx PCR PfGPx GLUTATHIONE PEROXIDASE MALARIA
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Summary:	In this paper we report the isolation and the characterization of a gene encoding the antioxidant enzyme glutathione peroxidase from the human malaria parasite Plasmodium falciparum. This gene contains two introns of 208 and 168 bp and is present in a single copy on chromosome 13. The open reading frame encodes a protein with a predicted length of 205 amino acids, which possesses a potential cleavage site between residues 21 and 22 after a hydrophobic region with the characteristics of a signal sequence. Therefore, the mature protein is predicted to be 184 residues long with a molecular mass of 21 404 Da. In comparison with other known glutathione peroxidases many amino acid residues implicated in catalysis are conserved in the malarial enzyme. Phylogenetic analysis indicates that the deduced protein sequence is more closely related to plant glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase. A 1.5-kb transcript was identified in asynchronous erythrocytic stages.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0166-6851 1872-9428
DOI:	10.1016/S0166-6851(96)02632-1