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J. Biol. Chem., Vol. 278, Issue 16, 14174-14184, April 18, 2003
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From the Eukaryotic mRNA capping enzymes are
bifunctional, carrying both RNA triphosphatase (RTPase) and
guanylyltransferase (GTase) activities. The Caenorhabditis
elegans CEL-1 capping enzyme consists of an N-terminal region
with RTPase activity and a C-terminal region that resembles known
GTases, However, CEL-1 has not previously been shown to have GTase
activity. Cloning of the cel-1 cDNA shows that the
full-length protein has 623 amino acids, including an additional 38 residues at the C termini and 12 residues at the N termini not
originally predicted from the genomic sequence. Full-length CEL-1 has
RTPase and GTase activities, and the cDNA can functionally replace
the capping enzyme genes in Saccharomyces cerevisiae. The
CEL-1 RTPase domain is related by sequence to protein-tyrosine
phosphatases; therefore, mutagenesis of residues predicted to be
important for RTPase activity was carried out. CEL-1 uses a mechanism
similar to protein-tyrosine phosphatases, except that there was not an
absolute requirement for a conserved acidic residue that acts as a
proton donor. CEL-1 shows a strong preference for RNA substrates of at
least three nucleotides in length. RNA-mediated interference in
C. elegans embryos shows that lack of CEL-1 causes
development to arrest with a phenotype similar to that seen when RNA
polymerase II elongation activity is disrupted. Therefore, capping is
essential for gene expression in metazoans.
The Caenorhabditis elegans
mRNA 5'-Capping Enzyme
IN VITRO AND IN VIVO CHARACTERIZATION*
§,
,**,,§§
Department of Biological Chemistry and
Molecular Pharmacology and ¶ Center for Blood Research and
Department of Pathology, Harvard Medical School,
Boston, Massachusetts 02115
*
This work was supported by National Institutes of Health
Grants GM56663 (to S. B.) and GM62891 (to T. K. B.).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.
Postdoctoral Fellow For Research Abroad of the Japan Society
for the Promotion of Science.
**
Present address: Mayo Clinic, Rochester, MN 55901.
Present address: Laboratory of Seeds Finding Technology, Eisai
Co., Ltd., Ibaraki 300-2635, Japan.
§§
A scholar of the Leukemia And Lymphoma Society. To whom
correspondence should be addressed: Dept. of Biological Chemistry and
Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave.,
Boston, MA 02115. Tel.: 617-432-0696; Fax: 617-738-0516; E-mail:
steveb@hms.harvard.edu.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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