Multiple Functionally Redundant Signals Mediate Targeting to the Apicoplast in the Apicomplexan Parasite Toxoplasma gondii

@article{Harb2004MultipleFR,
  title={Multiple Functionally Redundant Signals Mediate Targeting to the Apicoplast in the Apicomplexan Parasite Toxoplasma gondii},
  author={O. Harb and B. Chatterjee and M. Fraunholz and M. J. Crawford and M. Nishi and D. Roos},
  journal={Eukaryotic Cell},
  year={2004},
  volume={3},
  pages={663 - 674}
}
  • O. Harb, B. Chatterjee, +3 authors D. Roos
  • Published 2004
  • Biology, Medicine
  • Eukaryotic Cell
    • ABSTRACT Most species of the protozoan phylum Apicomplexa harbor an endosymbiotic organelle—the apicoplast—acquired when an ancestral parasite engulfed a eukaryotic plastid-containing alga. Several hundred proteins are encoded in the parasite nucleus and are posttranslationally targeted to the apicoplast by a distinctive bipartite signal. The N-terminal 20 to 30 amino acids of nucleus-encoded apicoplast targeted proteins function as a classical signal sequence, mediating entry into the… CONTINUE READING
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    References

    SHOWING 1-10 OF 69 REFERENCES
    Analysis of targeting sequences demonstrates that trafficking to the Toxoplasma gondii plastid branches off the secretory system.
    • 107
    • PDF
    Targeting and Processing of Nuclear-encoded Apicoplast Proteins in Plastid Segregation Mutants of Toxoplasma gondii*
    • 49
    • PDF
    Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway
    • 500
    Nuclear-encoded proteins target to the plastid in Toxoplasma gondii and Plasmodium falciparum.
    • 689
    • PDF
    Deciphering apicoplast targeting signals--feature extraction from nuclear-encoded precursors of Plasmodium falciparum apicoplast proteins.
    • 204
    • PDF
    Analysis of apicoplast targeting and transit peptide processing in Toxoplasma gondii by deletional and insertional mutagenesis.
    • 39
    CIS AND TRANS FACTORS INVOLVED IN APICOPLAST TARGETING IN TOXOPLASMA GONDII
    • 18
    A plastid organelle as a drug target in apicomplexan parasites
    • 550
    Mining the Plasmodium genome database to define organellar function: what does the apicoplast do?
    • 87
    • PDF
    Nuclear-encoded, plastid-targeted genes suggest a single common origin for apicomplexan and dinoflagellate plastids.
    • 414
    • PDF