Open AccessModification of the 5'-terminus of mRNA by soluble guanylyl and methyl transferases from vaccinia virus.
Author(s) -
M J Ensinger,
Scott A. Martin,
Enzo Paoletti,
Bernard Moss
Publication year - 1975
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.72.7.2525
Subject(s) - vaccinia , gtp' , messenger rna , virus , rna , enzyme , transferase , chemistry , biochemistry , methyltransferase , residue (chemistry) , nucleotide , biology , virology , methylation , gene , recombinant dna
RNA guanylyl and methyl transferases have been solubilized from vaccinia virus cores. The guanylyl transferase specifically adds a GMP residue to the 5'-terminus of unmethylated vaccinia virus mRNA to form the structures G(5')ppp(5')Gp- and G(5')ppp(5')Ap-. Studies with [alpha-32P]GTP and [beta, gamma-32P]GTP indicated that only the alpha-phosphate is transferred. In the presence of S-adenosylmethionine, the methyl transferases convert the blocked 5'-termini to m7G(5')ppp(5')Gmp- and m7G(5')ppp(5')Amp-. Similarly, the enzymes can modify synthetic poly(A) to form the structure m7G(5')ppp(5')Amp-.