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http://purl.uniprot.org/citations/12576476http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12576476http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/12576476http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m212101200"xsd:string
http://purl.uniprot.org/citations/12576476http://purl.uniprot.org/core/author"Takagi T."xsd:string
http://purl.uniprot.org/citations/12576476http://purl.uniprot.org/core/author"Buratowski S."xsd:string
http://purl.uniprot.org/citations/12576476http://purl.uniprot.org/core/author"Sawa C."xsd:string
http://purl.uniprot.org/citations/12576476http://purl.uniprot.org/core/author"Blackwell T.K."xsd:string
http://purl.uniprot.org/citations/12576476http://purl.uniprot.org/core/author"Walker A.K."xsd:string
http://purl.uniprot.org/citations/12576476http://purl.uniprot.org/core/author"Takase Y."xsd:string
http://purl.uniprot.org/citations/12576476http://purl.uniprot.org/core/author"Diehn F."xsd:string
http://purl.uniprot.org/citations/12576476http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12576476http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/12576476http://purl.uniprot.org/core/pages"14174-14184"xsd:string
http://purl.uniprot.org/citations/12576476http://purl.uniprot.org/core/title"The Caenorhabditis elegans mRNA 5'-capping enzyme. In vitro and in vivo characterization."xsd:string
http://purl.uniprot.org/citations/12576476http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12576476http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12576476
http://purl.uniprot.org/citations/12576476http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12576476
http://purl.uniprot.org/uniprot/Q17607#attribution-F1FF5E3A4D65659D0ED3144E550FCD1Bhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12576476
http://purl.uniprot.org/uniprot/#_Q17607-mappedCitation-12576476http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12576476
http://purl.uniprot.org/uniprot/#_Q6A3Q2-mappedCitation-12576476http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12576476
http://purl.uniprot.org/uniprot/Q17607http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12576476
http://purl.uniprot.org/uniprot/Q6A3Q2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12576476