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Eukaryotic Cell, August 2009, p. 1134-1145, Vol. 8, No. 8
1535-9778/09/$08.00+0     doi:10.1128/EC.00083-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

An Unusual ERAD-Like Complex Is Targeted to the Apicoplast of Plasmodium falciparum{triangledown} ,{dagger}

Simone Spork,1 Jan A. Hiss,2 Katharina Mandel,1 Maik Sommer,3,{ddagger} Taco W. A. Kooij,4 Trang Chu,1 Gisbert Schneider,2 Uwe G. Maier,3 and Jude M. Przyborski1*

Department of Parasitology, Faculty of Biology, Philipps University Marburg, Marburg, Germany,1 Institute of Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University, Siesmayerstrasse 70, 60323 Frankfurt, Germany,2 Laboratory for Cell Biology, Philipps University Marburg, Marburg, Germany,3 Department of Parasitology, Heidelberg University School of Medicine, Im Neuenheimer Feld 324, 69120 Heidelberg, Germany4

Received 12 March 2009/ Accepted 25 May 2009

Many apicomplexan parasites, including Plasmodium falciparum, harbor a so-called apicoplast, a complex plastid of red algal origin which was gained by a secondary endosymbiotic event. The exact molecular mechanisms directing the transport of nuclear-encoded proteins to the apicoplast of P. falciparum are not well understood. Recently, in silico analyses revealed a second copy of proteins homologous to components of the endoplasmic reticulum (ER)-associated protein degradation (ERAD) system in organisms with secondary plastids, including the malaria parasite P. falciparum. These proteins are predicted to be endowed with an apicoplast targeting signal and are suggested to play a role in the transport of nuclear-encoded proteins to the apicoplast. Here, we have studied components of this ERAD-derived putative preprotein translocon complex in malaria parasites. Using transfection technology coupled with fluorescence imaging techniques we can demonstrate that the N terminus of several ERAD-derived components targets green fluorescent protein to the apicoplast. Furthermore, we confirm that full-length PfsDer1-1 and PfsUba1 (homologues of yeast ERAD components) localize to the apicoplast, where PfsDer1-1 tightly associates with membranes. Conversely, PfhDer1-1 (a host-specific copy of the Der1-1 protein) localizes to the ER. Our data suggest that ERAD components have been "rewired" to provide a conduit for protein transport to the apicoplast. Our results are discussed in relation to the nature of the apicoplast protein transport machinery.

* Corresponding author. Mailing address: Department of Parasitology, Faculty of Biology, Karl von Frisch Strasse 8, 35043, Marburg, Germany. Phone: 49 6421 2826596. Fax: 49 6421 2821531. E-mail: przybors{at}staff.uni-marburg.de

{triangledown} Published ahead of print on 5 June 2009.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

{ddagger} Present address: Molekulare Zellbiologie der Pflanzen, Biozentrum N200, Max von Laue Str. 9, 60438 Frankfurt, Germany.

Eukaryotic Cell, August 2009, p. 1134-1145, Vol. 8, No. 8
1535-9778/09/$08.00+0     doi:10.1128/EC.00083-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Lim, L., McFadden, G. I. (2010). The evolution, metabolism and functions of the apicoplast. Phil Trans R Soc B 365: 749-763 [Abstract] [Full Text]  
  • Agrawal, S., van Dooren, G. G., Beatty, W. L., Striepen, B. (2009). Genetic Evidence that an Endosymbiont-derived Endoplasmic Reticulum-associated Protein Degradation (ERAD) System Functions in Import of Apicoplast Proteins. J. Biol. Chem. 284: 33683-33691 [Abstract] [Full Text]  


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