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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ho, C. K. Shuman, S. |
| Description | Author Affiliation: Ho CK ( Molecular Biology Program, Sloan-Kettering Institute, New York, NY 10021, USA.); |
| 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. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 6 |
| Volume Number | 98 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2001-03-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Acid Anhydride Hydrolases Metabolism Nucleotidyltransferases Plasmodium Falciparum Enzymology RNA Caps Biosynthesis RNA, Protozoan Genetics Isolation & Purification Adenosine Triphosphate Amino Acid Sequence Animals Guanosine Monophosphate Molecular Sequence Data Recombinant Fusion Proteins Saccharomyces Cerevisiae Sequence Homology, Amino Acid Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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