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MBE Advance Access published online on August 18, 2004
Molecular Biology and Evolution, doi:10.1093/molbev/msh233
Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2004; all rights reserved
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Accepted July 9, 2004

Original Article

Evolutionary Pressures on Apicoplast Transit Peptides

Stuart A. Ralph 1, Bernardo J. Foth 1, Neil Hall 2, Geoffrey I. McFadden 1*

1 PCBRC, School of Botany, University of Melbourne, Parkville, Victoria, 3010 Australia
2 The Wellcome Trust Sanger Institute, TheWellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SA

* To whom correspondence should be addressed. E-mail: gim{at}unimelb.edu.au.


  Abstract

Malaria parasites (species of the genus Plasmodium) harbour a relict chloroplast (the apicoplast) that is the target of novel anti-malarials. 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. 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.

Keywords: Plasmodium falciparum; plastid; apicoplast; targeting; transit peptide; nucleotide bias.
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