Cap-Specific mRNA (Nucleoside-O2'-)-Methyltransferase and Poly(A) Polymerase Stimulatory Activities of Vaccinia Virus are Mediated by a Single Protein

The vaccinia virus gene for S-adenosyl-L-methionine:mRNA (nucleoside-O2'-)-methyltransferase, an enzyme required for the formation of the 5' cap structure of mRNA, was identified. Protein sequence analysis revealed that this cap-specific methyltransferase is derived from the same open read...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1992-04, Vol.89 (7), p.2897-2901
Main Authors: Schnierle, Barabara S., Gershon, Paul D., Moss, Bernard
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biochemistry
Biological and medical sciences
Enzyme Activation
Enzymes
Eukaryotic cells
Fundamental and applied biological sciences. Psychology
Genes, Viral
Genetics
Medical research
Messenger RNA
Microbiology
Molecular Sequence Data
mRNA
mRNA (nucleoside-O super(2')-)-methyltransferase
NAD super(+) ADP-ribosyltransferase
Nucleosides
Nucleotidyltransferases - genetics
Nucleotidyltransferases - metabolism
Open reading frames
Polynucleotide Adenylyltransferase - metabolism
Proteins
Ribonucleic acid
RNA
RNA Caps - metabolism
RNA Processing, Post-Transcriptional
RNA, Messenger - metabolism
RNA, Viral - metabolism
Vaccinia
Vaccinia virus
Vaccinia virus - genetics
Vaccinia virus - metabolism
Viral Structural Proteins - genetics
Virology
Viruses
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Description
Summary:The vaccinia virus gene for S-adenosyl-L-methionine:mRNA (nucleoside-O2'-)-methyltransferase, an enzyme required for the formation of the 5' cap structure of mRNA, was identified. Protein sequence analysis revealed that this cap-specific methyltransferase is derived from the same open reading frame as that previously shown to encode VP39, a Mr39,000 dissociable subunit of poly(A) polymerase that stimulates the formation of long poly(A) tails. Consistent with this finding, methyltransferase activity was associated with the heterodimeric poly(A) polymerase, which is composed of VP55 and VP39 subunits, as well as with monomeric VP39 protein isolated from vaccinia virions. In addition, cap-specific nucleoside-O2'-methyltransferase activity is associated with recombinant VP39, which was purified to near homogeneity from mammalian cells. From these data, we concluded that the same protein functions as a methyltransferase and a poly(A) polymerase stimulatory factor to modify the 5' and 3' ends of mRNA, respectively
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.89.7.2897