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J Biol Chem, Vol. 273, Issue 34, 21443-21446, August 21, 1998
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From the Guanine 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 in the
bifunctional mammalian capping enzyme. Binding studies demonstrated
that the human cap methyltransferase associated with recombinant
capping enzyme. Consistent with selective capping of RNA polymerase II transcripts, methyltransferase also formed ternary complexes with capping enzyme and the elongating form of RNA polymerase II.
Center for Advanced Biotechnology and
Medicine, Piscataway, New Jersey 08854-5638 and the ¶ Programa de
Biologia Celular y Molecular, Instituto de Ciencias Biomedicas,
Facultad de Medicina, Universidad de Chile, Casilla 70086, Santiago 7, Chile
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