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Originally published In Press as doi:10.1074/jbc.M102000200 on April 23, 2001

J. Biol. Chem., Vol. 276, Issue 30, 28436-28442, July 27, 2001
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Targeting and Processing of Nuclear-encoded Apicoplast Proteins in Plastid Segregation Mutants of Toxoplasma gondii*

Cynthia Y. HeDagger , Boris StriepenDagger §, Charles H. Pletcher, John M. Murray||, and David S. RoosDagger **

From the Dagger  Department of Biology,  Cancer Center Flow Cytometry Shared Resource, and || Department of Cell Biology, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104

The apicoplast is a distinctive organelle associated with apicomplexan parasites, including Plasmodium sp. (which cause malaria) and Toxoplasma gondii (the causative agent of toxoplasmosis). This unusual structure (acquired by the engulfment of an ancestral alga and retention of the algal plastid) is essential for long-term parasite survival. Similar to other endosymbiotic organelles (mitochondria, chloroplasts), the apicoplast contains proteins that are encoded in the nucleus and post-translationally imported. Translocation across the four membranes surrounding the apicoplast is mediated by an N-terminal bipartite targeting sequence. Previous studies have described a recombinant "poison" that blocks plastid segregation during mitosis, producing parasites that lack an apicoplast and siblings containing a gigantic, nonsegregating plastid. To learn more about this remarkable phenomenon, we examined the localization and processing of the protein produced by this construct. Taking advantage of the ability to isolate apicoplast segregation mutants, we also demonstrated that processing of the transit peptide of nuclear-encoded apicoplast proteins requires plastid-associated activity.

* This work was supported by grants from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: Center for Tropical and Emerging Global Diseases and Dept. of Cellular Biology, University of Georgia, Athens, GA 30602.

** A Burroughs Wellcome Scholar in Molecular Parasitology. To whom correspondence should be addressed: Dept. of Biology, 305 Goddard Laboratories, University of Pennsylvania, Philadelphia, PA 19104-6018; Tel.: 215-898-2118; Fax: 215-898-8780; E-mail: droos@ mail.sas.upenn.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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