The Experts below are selected from a list of 162 Experts worldwide ranked by ideXlab platform

Stuart A Ralph - One of the best experts on this subject based on the ideXlab platform.

  • a dual targeted aminoacyl trna synthetase in plasmodium falciparum charges cytosolic and Apicoplast trnacys
    Biochemical Journal, 2014
    Co-Authors: James Pham, Reiko Sakaguchi, Lee M Yeoh, Nilushi S De Silva, Geoffrey I Mcfadden, Stuart A Ralph
    Abstract:

    Plasmodium parasites possess two endosymbiotic organelles: a mitochondrion and a relict plastid called the Apicoplast. To accommodate the translational requirements of these organelles in addition to its cytosolic translation apparatus, the parasite must maintain a supply of charged tRNA molecules in each of these compartments. In the present study we investigate how the parasite manages these translational requirements for charged tRNACys with only a single gene for CysRS (cysteinyl-tRNA synthetase). We demonstrate that the single Pf CysRS ( Plasmodium falciparum CysRS) transcript is alternatively spliced, and, using a combination of endogenous and heterologous tagging experiments in both P. falciparum and Toxoplasma gondii , we show that CysRS isoforms traffic to the cytosol and Apicoplast. Pf CysRS can recognize and charge the eukaryotic tRNACys encoded by the Plasmodium nucleus as well as the bacterial-type tRNA encoded by the Apicoplast Genome, albeit with a preference for the eukaryotic type cytosolic tRNA. The results of the present study indicate that apicomplexan parasites have lost their original plastidic cysteinyl-tRNA synthetase, and have replaced it with a dual-targeted eukaryotic type CysRS that recognizes plastid and nuclear tRNACys. Inhibitors of the Plasmodium dual-targeted CysRS would potentially offer a therapy capable of the desirable immediate effects on parasite growth as well as the irreversibility of inhibitors that disrupt Apicoplast inheritance. Abbreviations: aaRS, aminoacyl-tRNA synthetase; ACP, acyl carrier protein; CRT, chloroquine-resistance transporter; CysRS, cysteinyl-tRNA synthetase; HA, haemagluttinin; PfCysRS, Plasmodium falciparum CysRS; TgCysRS, Toxoplasma gondii CysRS

  • a dual targeted aminoacyl trna synthetase in plasmodium falciparum charges cytosolic and Apicoplast trnacys
    Biochemical Journal, 2014
    Co-Authors: James Pham, Reiko Sakaguchi, Lee M Yeoh, Nilushi S De Silva, Geoffrey I Mcfadden, Yaming Hou, Stuart A Ralph
    Abstract:

    Plasmodium parasites possess two endosymbiotic organelles: a mitochondrion and a relict plastid called the Apicoplast. To accommodate the translational requirements of these organelles in addition to its cytosolic translation apparatus, the parasite must maintain a supply of charged tRNA molecules in each of these compartments. In the present study we investigate how the parasite manages these translational requirements for charged tRNACys with only a single gene for CysRS (cysteinyl-tRNA synthetase). We demonstrate that the single PfCysRS (Plasmodium falciparum CysRS) transcript is alternatively spliced, and, using a combination of endogenous and heterologous tagging experiments in both P. falciparum and Toxoplasma gondii, we show that CysRS isoforms traffic to the cytosol and Apicoplast. PfCysRS can recognize and charge the eukaryotic tRNACys encoded by the Plasmodium nucleus as well as the bacterial-type tRNA encoded by the Apicoplast Genome, albeit with a preference for the eukaryotic type cytosolic tRNA. The results of the present study indicate that apicomplexan parasites have lost their original plastidic cysteinyl-tRNA synthetase, and have replaced it with a dual-targeted eukaryotic type CysRS that recognizes plastid and nuclear tRNACys. Inhibitors of the Plasmodium dual-targeted CysRS would potentially offer a therapy capable of the desirable immediate effects on parasite growth as well as the irreversibility of inhibitors that disrupt Apicoplast inheritance.

James Pham - One of the best experts on this subject based on the ideXlab platform.

  • a dual targeted aminoacyl trna synthetase in plasmodium falciparum charges cytosolic and Apicoplast trnacys
    Biochemical Journal, 2014
    Co-Authors: James Pham, Reiko Sakaguchi, Lee M Yeoh, Nilushi S De Silva, Geoffrey I Mcfadden, Stuart A Ralph
    Abstract:

    Plasmodium parasites possess two endosymbiotic organelles: a mitochondrion and a relict plastid called the Apicoplast. To accommodate the translational requirements of these organelles in addition to its cytosolic translation apparatus, the parasite must maintain a supply of charged tRNA molecules in each of these compartments. In the present study we investigate how the parasite manages these translational requirements for charged tRNACys with only a single gene for CysRS (cysteinyl-tRNA synthetase). We demonstrate that the single Pf CysRS ( Plasmodium falciparum CysRS) transcript is alternatively spliced, and, using a combination of endogenous and heterologous tagging experiments in both P. falciparum and Toxoplasma gondii , we show that CysRS isoforms traffic to the cytosol and Apicoplast. Pf CysRS can recognize and charge the eukaryotic tRNACys encoded by the Plasmodium nucleus as well as the bacterial-type tRNA encoded by the Apicoplast Genome, albeit with a preference for the eukaryotic type cytosolic tRNA. The results of the present study indicate that apicomplexan parasites have lost their original plastidic cysteinyl-tRNA synthetase, and have replaced it with a dual-targeted eukaryotic type CysRS that recognizes plastid and nuclear tRNACys. Inhibitors of the Plasmodium dual-targeted CysRS would potentially offer a therapy capable of the desirable immediate effects on parasite growth as well as the irreversibility of inhibitors that disrupt Apicoplast inheritance. Abbreviations: aaRS, aminoacyl-tRNA synthetase; ACP, acyl carrier protein; CRT, chloroquine-resistance transporter; CysRS, cysteinyl-tRNA synthetase; HA, haemagluttinin; PfCysRS, Plasmodium falciparum CysRS; TgCysRS, Toxoplasma gondii CysRS

  • a dual targeted aminoacyl trna synthetase in plasmodium falciparum charges cytosolic and Apicoplast trnacys
    Biochemical Journal, 2014
    Co-Authors: James Pham, Reiko Sakaguchi, Lee M Yeoh, Nilushi S De Silva, Geoffrey I Mcfadden, Yaming Hou, Stuart A Ralph
    Abstract:

    Plasmodium parasites possess two endosymbiotic organelles: a mitochondrion and a relict plastid called the Apicoplast. To accommodate the translational requirements of these organelles in addition to its cytosolic translation apparatus, the parasite must maintain a supply of charged tRNA molecules in each of these compartments. In the present study we investigate how the parasite manages these translational requirements for charged tRNACys with only a single gene for CysRS (cysteinyl-tRNA synthetase). We demonstrate that the single PfCysRS (Plasmodium falciparum CysRS) transcript is alternatively spliced, and, using a combination of endogenous and heterologous tagging experiments in both P. falciparum and Toxoplasma gondii, we show that CysRS isoforms traffic to the cytosol and Apicoplast. PfCysRS can recognize and charge the eukaryotic tRNACys encoded by the Plasmodium nucleus as well as the bacterial-type tRNA encoded by the Apicoplast Genome, albeit with a preference for the eukaryotic type cytosolic tRNA. The results of the present study indicate that apicomplexan parasites have lost their original plastidic cysteinyl-tRNA synthetase, and have replaced it with a dual-targeted eukaryotic type CysRS that recognizes plastid and nuclear tRNACys. Inhibitors of the Plasmodium dual-targeted CysRS would potentially offer a therapy capable of the desirable immediate effects on parasite growth as well as the irreversibility of inhibitors that disrupt Apicoplast inheritance.

Reiko Sakaguchi - One of the best experts on this subject based on the ideXlab platform.

  • a dual targeted aminoacyl trna synthetase in plasmodium falciparum charges cytosolic and Apicoplast trnacys
    Biochemical Journal, 2014
    Co-Authors: James Pham, Reiko Sakaguchi, Lee M Yeoh, Nilushi S De Silva, Geoffrey I Mcfadden, Stuart A Ralph
    Abstract:

    Plasmodium parasites possess two endosymbiotic organelles: a mitochondrion and a relict plastid called the Apicoplast. To accommodate the translational requirements of these organelles in addition to its cytosolic translation apparatus, the parasite must maintain a supply of charged tRNA molecules in each of these compartments. In the present study we investigate how the parasite manages these translational requirements for charged tRNACys with only a single gene for CysRS (cysteinyl-tRNA synthetase). We demonstrate that the single Pf CysRS ( Plasmodium falciparum CysRS) transcript is alternatively spliced, and, using a combination of endogenous and heterologous tagging experiments in both P. falciparum and Toxoplasma gondii , we show that CysRS isoforms traffic to the cytosol and Apicoplast. Pf CysRS can recognize and charge the eukaryotic tRNACys encoded by the Plasmodium nucleus as well as the bacterial-type tRNA encoded by the Apicoplast Genome, albeit with a preference for the eukaryotic type cytosolic tRNA. The results of the present study indicate that apicomplexan parasites have lost their original plastidic cysteinyl-tRNA synthetase, and have replaced it with a dual-targeted eukaryotic type CysRS that recognizes plastid and nuclear tRNACys. Inhibitors of the Plasmodium dual-targeted CysRS would potentially offer a therapy capable of the desirable immediate effects on parasite growth as well as the irreversibility of inhibitors that disrupt Apicoplast inheritance. Abbreviations: aaRS, aminoacyl-tRNA synthetase; ACP, acyl carrier protein; CRT, chloroquine-resistance transporter; CysRS, cysteinyl-tRNA synthetase; HA, haemagluttinin; PfCysRS, Plasmodium falciparum CysRS; TgCysRS, Toxoplasma gondii CysRS

  • a dual targeted aminoacyl trna synthetase in plasmodium falciparum charges cytosolic and Apicoplast trnacys
    Biochemical Journal, 2014
    Co-Authors: James Pham, Reiko Sakaguchi, Lee M Yeoh, Nilushi S De Silva, Geoffrey I Mcfadden, Yaming Hou, Stuart A Ralph
    Abstract:

    Plasmodium parasites possess two endosymbiotic organelles: a mitochondrion and a relict plastid called the Apicoplast. To accommodate the translational requirements of these organelles in addition to its cytosolic translation apparatus, the parasite must maintain a supply of charged tRNA molecules in each of these compartments. In the present study we investigate how the parasite manages these translational requirements for charged tRNACys with only a single gene for CysRS (cysteinyl-tRNA synthetase). We demonstrate that the single PfCysRS (Plasmodium falciparum CysRS) transcript is alternatively spliced, and, using a combination of endogenous and heterologous tagging experiments in both P. falciparum and Toxoplasma gondii, we show that CysRS isoforms traffic to the cytosol and Apicoplast. PfCysRS can recognize and charge the eukaryotic tRNACys encoded by the Plasmodium nucleus as well as the bacterial-type tRNA encoded by the Apicoplast Genome, albeit with a preference for the eukaryotic type cytosolic tRNA. The results of the present study indicate that apicomplexan parasites have lost their original plastidic cysteinyl-tRNA synthetase, and have replaced it with a dual-targeted eukaryotic type CysRS that recognizes plastid and nuclear tRNACys. Inhibitors of the Plasmodium dual-targeted CysRS would potentially offer a therapy capable of the desirable immediate effects on parasite growth as well as the irreversibility of inhibitors that disrupt Apicoplast inheritance.

Lee M Yeoh - One of the best experts on this subject based on the ideXlab platform.

  • a dual targeted aminoacyl trna synthetase in plasmodium falciparum charges cytosolic and Apicoplast trnacys
    Biochemical Journal, 2014
    Co-Authors: James Pham, Reiko Sakaguchi, Lee M Yeoh, Nilushi S De Silva, Geoffrey I Mcfadden, Stuart A Ralph
    Abstract:

    Plasmodium parasites possess two endosymbiotic organelles: a mitochondrion and a relict plastid called the Apicoplast. To accommodate the translational requirements of these organelles in addition to its cytosolic translation apparatus, the parasite must maintain a supply of charged tRNA molecules in each of these compartments. In the present study we investigate how the parasite manages these translational requirements for charged tRNACys with only a single gene for CysRS (cysteinyl-tRNA synthetase). We demonstrate that the single Pf CysRS ( Plasmodium falciparum CysRS) transcript is alternatively spliced, and, using a combination of endogenous and heterologous tagging experiments in both P. falciparum and Toxoplasma gondii , we show that CysRS isoforms traffic to the cytosol and Apicoplast. Pf CysRS can recognize and charge the eukaryotic tRNACys encoded by the Plasmodium nucleus as well as the bacterial-type tRNA encoded by the Apicoplast Genome, albeit with a preference for the eukaryotic type cytosolic tRNA. The results of the present study indicate that apicomplexan parasites have lost their original plastidic cysteinyl-tRNA synthetase, and have replaced it with a dual-targeted eukaryotic type CysRS that recognizes plastid and nuclear tRNACys. Inhibitors of the Plasmodium dual-targeted CysRS would potentially offer a therapy capable of the desirable immediate effects on parasite growth as well as the irreversibility of inhibitors that disrupt Apicoplast inheritance. Abbreviations: aaRS, aminoacyl-tRNA synthetase; ACP, acyl carrier protein; CRT, chloroquine-resistance transporter; CysRS, cysteinyl-tRNA synthetase; HA, haemagluttinin; PfCysRS, Plasmodium falciparum CysRS; TgCysRS, Toxoplasma gondii CysRS

  • a dual targeted aminoacyl trna synthetase in plasmodium falciparum charges cytosolic and Apicoplast trnacys
    Biochemical Journal, 2014
    Co-Authors: James Pham, Reiko Sakaguchi, Lee M Yeoh, Nilushi S De Silva, Geoffrey I Mcfadden, Yaming Hou, Stuart A Ralph
    Abstract:

    Plasmodium parasites possess two endosymbiotic organelles: a mitochondrion and a relict plastid called the Apicoplast. To accommodate the translational requirements of these organelles in addition to its cytosolic translation apparatus, the parasite must maintain a supply of charged tRNA molecules in each of these compartments. In the present study we investigate how the parasite manages these translational requirements for charged tRNACys with only a single gene for CysRS (cysteinyl-tRNA synthetase). We demonstrate that the single PfCysRS (Plasmodium falciparum CysRS) transcript is alternatively spliced, and, using a combination of endogenous and heterologous tagging experiments in both P. falciparum and Toxoplasma gondii, we show that CysRS isoforms traffic to the cytosol and Apicoplast. PfCysRS can recognize and charge the eukaryotic tRNACys encoded by the Plasmodium nucleus as well as the bacterial-type tRNA encoded by the Apicoplast Genome, albeit with a preference for the eukaryotic type cytosolic tRNA. The results of the present study indicate that apicomplexan parasites have lost their original plastidic cysteinyl-tRNA synthetase, and have replaced it with a dual-targeted eukaryotic type CysRS that recognizes plastid and nuclear tRNACys. Inhibitors of the Plasmodium dual-targeted CysRS would potentially offer a therapy capable of the desirable immediate effects on parasite growth as well as the irreversibility of inhibitors that disrupt Apicoplast inheritance.

Nilushi S De Silva - One of the best experts on this subject based on the ideXlab platform.

  • a dual targeted aminoacyl trna synthetase in plasmodium falciparum charges cytosolic and Apicoplast trnacys
    Biochemical Journal, 2014
    Co-Authors: James Pham, Reiko Sakaguchi, Lee M Yeoh, Nilushi S De Silva, Geoffrey I Mcfadden, Stuart A Ralph
    Abstract:

    Plasmodium parasites possess two endosymbiotic organelles: a mitochondrion and a relict plastid called the Apicoplast. To accommodate the translational requirements of these organelles in addition to its cytosolic translation apparatus, the parasite must maintain a supply of charged tRNA molecules in each of these compartments. In the present study we investigate how the parasite manages these translational requirements for charged tRNACys with only a single gene for CysRS (cysteinyl-tRNA synthetase). We demonstrate that the single Pf CysRS ( Plasmodium falciparum CysRS) transcript is alternatively spliced, and, using a combination of endogenous and heterologous tagging experiments in both P. falciparum and Toxoplasma gondii , we show that CysRS isoforms traffic to the cytosol and Apicoplast. Pf CysRS can recognize and charge the eukaryotic tRNACys encoded by the Plasmodium nucleus as well as the bacterial-type tRNA encoded by the Apicoplast Genome, albeit with a preference for the eukaryotic type cytosolic tRNA. The results of the present study indicate that apicomplexan parasites have lost their original plastidic cysteinyl-tRNA synthetase, and have replaced it with a dual-targeted eukaryotic type CysRS that recognizes plastid and nuclear tRNACys. Inhibitors of the Plasmodium dual-targeted CysRS would potentially offer a therapy capable of the desirable immediate effects on parasite growth as well as the irreversibility of inhibitors that disrupt Apicoplast inheritance. Abbreviations: aaRS, aminoacyl-tRNA synthetase; ACP, acyl carrier protein; CRT, chloroquine-resistance transporter; CysRS, cysteinyl-tRNA synthetase; HA, haemagluttinin; PfCysRS, Plasmodium falciparum CysRS; TgCysRS, Toxoplasma gondii CysRS

  • a dual targeted aminoacyl trna synthetase in plasmodium falciparum charges cytosolic and Apicoplast trnacys
    Biochemical Journal, 2014
    Co-Authors: James Pham, Reiko Sakaguchi, Lee M Yeoh, Nilushi S De Silva, Geoffrey I Mcfadden, Yaming Hou, Stuart A Ralph
    Abstract:

    Plasmodium parasites possess two endosymbiotic organelles: a mitochondrion and a relict plastid called the Apicoplast. To accommodate the translational requirements of these organelles in addition to its cytosolic translation apparatus, the parasite must maintain a supply of charged tRNA molecules in each of these compartments. In the present study we investigate how the parasite manages these translational requirements for charged tRNACys with only a single gene for CysRS (cysteinyl-tRNA synthetase). We demonstrate that the single PfCysRS (Plasmodium falciparum CysRS) transcript is alternatively spliced, and, using a combination of endogenous and heterologous tagging experiments in both P. falciparum and Toxoplasma gondii, we show that CysRS isoforms traffic to the cytosol and Apicoplast. PfCysRS can recognize and charge the eukaryotic tRNACys encoded by the Plasmodium nucleus as well as the bacterial-type tRNA encoded by the Apicoplast Genome, albeit with a preference for the eukaryotic type cytosolic tRNA. The results of the present study indicate that apicomplexan parasites have lost their original plastidic cysteinyl-tRNA synthetase, and have replaced it with a dual-targeted eukaryotic type CysRS that recognizes plastid and nuclear tRNACys. Inhibitors of the Plasmodium dual-targeted CysRS would potentially offer a therapy capable of the desirable immediate effects on parasite growth as well as the irreversibility of inhibitors that disrupt Apicoplast inheritance.