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

Proc Natl Acad Sci U S A. 1975 Jul;72(7):2525-9. doi: 10.1073/pnas.72.7.2525.

Abstract

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-.

MeSH terms

  • Calcium / pharmacology
  • Chromatography, DEAE-Cellulose
  • Enzyme Activation / drug effects
  • Guanine Nucleotides
  • Kinetics
  • Magnesium / pharmacology
  • Manganese / pharmacology
  • Methyltransferases / metabolism*
  • RNA Nucleotidyltransferases / metabolism*
  • RNA, Messenger / metabolism*
  • RNA, Viral / metabolism*
  • S-Adenosylmethionine / metabolism
  • Vaccinia virus / enzymology*

Substances

  • Guanine Nucleotides
  • RNA, Messenger
  • RNA, Viral
  • Manganese
  • S-Adenosylmethionine
  • Methyltransferases
  • RNA Nucleotidyltransferases
  • Magnesium
  • Calcium