Traffic. 2015 Sep 18. doi: 10.1111/tra.12333. [Epub ahead of print]
Sheiner L1,2,
Fellows JD1,
Ovciarikova J2,
Brooks CF1,
Agrawal S1,
Holmes ZC1,
Bietz I3,
Flinner N4,
Heiny S3,
Mirus O4,
Przyborski JM3,
Striepen B1.
Abstract
Apicomplexa are unicellular parasites causing important human and animal diseases, including malaria and toxoplasmosis. Most of these pathogens possess a relict but essential plastid, the apicoplast. The apicoplast was acquired by secondary endosymbiosis between a red alga and a flagellated eukaryotic protist. As a result the apicoplast is surrounded by four membranes. This complex structure necessitates a system of transport signals and translocons allowing nuclear encoded proteins to find their way to specific apicoplast sub-compartments. Previous studies identified translocons traversing two of the four apicoplast membranes. Here we provide functional support for the role of an apicomplexan Toc75 homolog in apicoplast protein transport. We identify two apicomplexan genes encoding Toc75 and Sam50, both members of the Omp85 protein family. We localize the respective proteins to the apicoplast and the mitochondrion of Toxoplasma and Plasmodium. We show that the Toxoplasma Toc75 is essential for parasite growth and that its depletion results in a rapid defect in the import of apicoplast stromal proteins while the import of proteins of the outer compartments is affected only as the secondary consequence of organelle loss. These observations along with the homology to Toc75 suggest a potential role in transport through the second innermost membrane.
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KEYWORDS:
Apicomplexa; Omp85; Plasmodium; Sam50; Toc75; Toxoplasma; apicoplast; complex plastid; protein trafficking
- PMID:
- 26381927
- [PubMed - as supplied by publisher]
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