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 |