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Authordc.contributor.authorPillutla, Renuka C. 
Authordc.contributor.authorYue, Zhenyu 
Authordc.contributor.authorMaldonado, Edio 
Authordc.contributor.authorShatkin, Aaron J. 
Cita de ítemdc.identifier.citationJournal of Biological Chemistry, Volumen 273, Issue 34, 2018, Pages 21443-21446
Abstractdc.description.abstractGuanine N-7 methylation is an essential step in the formation of the m7GpppN cap structure that is characteristic of eukaryotic mRNA 5' ends. The terminal 7-methylguanosine is recognized by cap-binding proteins that facilitate key events in gene expression including mRNA processing, transport, and translation. Here we describe the cloning, primary structure, and properties of human RNA (guanine-7-)methyltransferase. Sequence alignment of the 476-amino acid human protein with the corresponding yeast ABD1 enzyme demonstrated the presence of several conserved motifs known to be required for methyltransferase activity. We also identified a Drosophila open reading frame that encodes a putative RNA (guanine-7-)methyltransferase and contains these motifs. Recombinant human methyltransferase transferred a methyl group from S-adenosylmethionine to GpppG 5'ends, which are formed on RNA polymerase II transcripts by the sequential action of RNA 5'-triphosphatase and guanylyltransferase activities
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link to Licensedc.rights.uri
Sourcedc.sourceJournal of Biological Chemistry
Keywordsdc.subjectMolecular Biology
Keywordsdc.subjectCell Biology
Títulodc.titleRecombinant human mRNA cap methyltransferase binds capping enzyme/RNA polymerase IIo complexes
Document typedc.typeArtículo de revista
dcterms.accessRightsdcterms.accessRightsAcceso Abierto
Indexationuchile.indexArtículo de publicación SCOPUS

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Attribution-NonCommercial-NoDerivs 3.0 Chile
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile