A yeast-like mRNA capping apparatus in Plasmodium falciparum Journal Article


Authors: Ho, C. K.; Shuman, S.
Article Title: A yeast-like mRNA capping apparatus in Plasmodium falciparum
Abstract: Analysis of the mRNA capping apparatus of the malaria parasite Plasmodium falciparum illuminates an evolutionary connection to fungi rather than metazoans. We show that P. falciparum encodes separate RNA guanylyltransferase (Pgt1) and RNA triphosphatase (Prt1) enzymes and that the triphosphatase component is a member of the fungal/viral family of metal-dependent phosphohydrolases, which are structurally and mechanistically unrelated to the cysteine-phosphatase-type RNA triphosphatases found in metazoans and plants. These results highlight the potential for discovery of mechanism-based antimalarial drugs designed to specifically block the capping of Plasmodium mRNAs. A simple heuristic scheme of eukaryotic phylogeny is suggested based on the structure and physical linkage of the triphosphatase and guanylyltransferase enzymes that catalyze cap formation.
Keywords: nonhuman; animals; phosphatase; acid anhydride hydrolases; amino acid sequence; molecular sequence data; sequence homology, amino acid; recombinant fusion proteins; messenger rna; enzyme analysis; saccharomyces cerevisiae; rna caps; eukaryota; yeast; adenosine triphosphate; antimalarial agent; plasmodium falciparum; enzyme structure; fungi; enzyme mechanism; eukaryote; metazoa; phylogeny; rna capping; nucleotidyltransferases; transferase; rna, protozoan; 5'-guanylic acid; humans; priority journal; article
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 98
Issue: 6
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 2001-03-13
Start Page: 3050
End Page: 3055
Language: English
DOI: 10.1073/pnas.061636198
PUBMED: 11248030
PROVIDER: scopus
PMCID: PMC30605
DOI/URL:
Notes: Export Date: 21 May 2015 -- Source: Scopus
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  1. Chong-Kiong Ho
    33 Ho
  2. Stewart H Shuman
    546 Shuman