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MBE Advance Access originally published online on August 18, 2004
Molecular Biology and Evolution 2004 21(12):2183-2194; doi:10.1093/molbev/msh233
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Molecular Biology and Evolution vol. 21 no. 12 © Society for Molecular Biology and Evolution 2004; all rights reserved.

Research Article

Evolutionary Pressures on Apicoplast Transit Peptides

Stuart A. Ralph*,1, Bernardo J. Foth*,2, Neil Hall{dagger},3 and Geoffrey I. McFadden*

* Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, Victoria, Australia; and {dagger} The Wellcome Trust Sanger Institute, The Wellcome Trust Genome Campus, Hinxton, Cambridge, UK

E-mail: gim{at}unimelb.edu.au.

Malaria parasites (species of the genus Plasmodium) harbor a relict chloroplast (the apicoplast) that is the target of novel antimalarials. Numerous nuclear-encoded proteins are translocated into the apicoplast courtesy of a bipartite N-terminal extension. The first component of the bipartite leader resembles a standard signal peptide present at the N-terminus of secreted proteins that enter the endomembrane system. Analysis of the second portion of the bipartite leaders of P. falciparum, the so-called transit peptide, indicates similarities to plant transit peptides, although the amino acid composition of P. falciparum transit peptides shows a strong bias, which we rationalize by the extraordinarily high AT content of P. falciparum DNA. 786 plastid transit peptides were also examined from several other apicomplexan parasites, as well as from angiosperm plants. In each case, amino acid biases were correlated with nucleotide AT content. A comparison of a spectrum of organisms containing primary and secondary plastids also revealed features unique to secondary plastid transit peptides. These unusual features are explained in the context of secondary plastid trafficking via the endomembrane system.

Key Words: Plasmodium falciparum • plastid • apicoplast • targeting • transit peptide • nucleotide bias


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