Modification of the 5'-terminus of mRNA by soluble guanylyl and methyl transferases from vaccinia virus. | Zendy

M J Ensinger | Zendy; Scott A. Martin | Zendy; Enzo Paoletti | Zendy; Bernard Moss | Zendy

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Modification 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

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-.

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