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Nucleic Acids Research 2006 34(2):496-505; doi:10.1093/nar/gkj450
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Published online 20 January 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
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Article

The Plasmodium selenoproteome

Alexey V. Lobanov1, Cesar Delgado1,2, Stefan Rahlfs3, Sergey V. Novoselov1, Gregory V. Kryukov1, Stephan Gromer4, Dolph L. Hatfield5, Katja Becker3 and Vadim N. Gladyshev1,*

1Department of Biochemistry, University of Nebraska Lincoln, NE 68588, USA 2Department of Computer Science, University of Nebraska Lincoln, NE 68588, USA 3Interdisziplinäres Forschungszentrum, Justus-Liebig University Giessen Heinrich-Buff-Ring 26-32, D-35392 Giessen, Germany 4Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 504 D-69120 Heidelberg, Germany 5Molecular Biology of Selenium Section, Laboratory of Cancer Prevention, National Cancer Institute, National Institutes of Health Bethesda, MD 20892, USA

*To whom correspondence should be addressed. Tel: +1 402 472 4948; Fax: +1 402 472 7842; Email: vgladyshev1{at}unl.edu

Received August 22, 2005. Revised October 3, 2005. Accepted January 3, 2006.

The use of selenocysteine (Sec) as the 21st amino acid in the genetic code has been described in all three major domains of life. However, within eukaryotes, selenoproteins are only known in animals and algae. In this study, we characterized selenoproteomes and Sec insertion systems in protozoan Apicomplexa parasites. We found that among these organisms, Plasmodium and Toxoplasma utilized Sec, whereas Cryptosporidium did not. However, Plasmodium had no homologs of known selenoproteins. By searching computationally for evolutionarily conserved selenocysteine insertion sequence (SECIS) elements, which are RNA structures involved in Sec insertion, we identified four unique Plasmodium falciparum selenoprotein genes. These selenoproteins were incorrectly annotated in PlasmoDB, were conserved in other Plasmodia and had no detectable homologs in other species. We provide evidence that two Plasmodium SECIS elements supported Sec insertion into parasite and endogenous selenoproteins when they were expressed in mammalian cells, demonstrating that the Plasmodium SECIS elements are functional and indicating conservation of Sec insertion between Apicomplexa and animals. Dependence of the plasmodial parasites on selenium suggests possible strategies for antimalarial drug development.


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