Abstract: 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.