EC Accepts, published online ahead of print on 5 June 2009

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Eukaryotic Cell doi:10.1128/EC.00083-09
Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

An unusual ERAD-like complex is targeted to the apicoplast of Plasmodium falciparum

Simone Spork, Jan A. Hiss, Katharina Mandel, Maik Sommer, Taco W.A. Kooij, Trang Chu, Gisbert Schneider, Uwe G. Maier, and Jude M. Przyborski^*

Department of Parasitology, Faculty of Biology, Philipps University Marburg, Marburg, Germany; Institute of Organic Chemistry & Chemical Biology, Johann Wolfgang Goethe-University, Siesmayerstr. 70, 60323 Frankfurt, Germany; Laboratory for Cell Biology, Philipps-University Marburg, Marburg, Germany; Department of Parasitology, Heidelberg University School of Medicine, Im Neuenheimer Feld 324, 69120 Heidelberg, Germany

^* To whom correspondence should be addressed. Email: przybors{at}staff.uni-marburg.de.

Many apicomplexan parasites, including Plasmodium falciparum, harbour 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 homologuous to components of the 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 pre-protein 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 GFP to the apicoplast. Furthermore, we confirm that full-length PfsDer1-1 and PfsUba1 (homologues of yeast ERAD components) localise to the apicoplast, where PfsDer1-1 tightly associates with membranes. Constantly, PfhDer1-1 localises to the endoplasmic reticulum. Our data suggests that ERAD components have been "re-wired" 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.

This article has been cited by other articles:

• 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]