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J. Biol. Chem., Vol. 277, Issue 1, 96-103, January 4, 2002
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From the A scheme of eukaryotic phylogeny has been
suggested based on the structure and physical linkage of the enzymes
that catalyze mRNA cap formation. Here we show that
the intracellular parasite Encephalitozoon cuniculi encodes
a complete mRNA capping apparatus consisting of separate
triphosphatase (EcCet1), guanylyltransferase (EcCeg1), and
methyltransferase (Ecm1) enzymes, which we characterize biochemically
and genetically. The triphosphatase EcCet1 belongs to a
metal-dependent phosphohydrolase family that includes the triphosphatase components of the capping apparatus of fungi, DNA viruses, and the malaria parasite Plasmodium
falciparum. These enzymes are structurally and
mechanistically unrelated to the metal-independent cysteine
phosphatase-type RNA triphosphatases found in metazoans and plants.
Our findings support the proposed evolutionary connection between
microsporidia and fungi, and they place fungi and protozoa in a common
lineage distinct from that of metazoans and plants. RNA
triphosphatase presents an attractive target for
antiprotozoal/antifungal drug development.
Characterization of the mRNA Capping Apparatus of the
Microsporidian Parasite Encephalitozoon cuniculi*
,¶
Molecular Biology Program, Sloan-Kettering
Institute, New York, New York 10021 and
§ Université Blaise Pascal, Clermont-Ferrand,
Aubière Cedex 63177, France
*
This work was supported in part by National Institutes of
Health Grant GM52470 (to S. S.) and Postdoctoral Fellowship
83A-061189 from the Swiss National Science Foundation (to S. H.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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