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      Importance of 5'-terminal blocking structure to stabilize mRNA in eukaryotic protein synthesis.

      Proceedings of the National Academy of Sciences of the United States of America
      Animals, Base Sequence, Cell-Free System, Exonucleases, metabolism, Globins, biosynthesis, Guanine Nucleotides, Insect Viruses, Peptide Chain Initiation, Translational, Phosphoric Diester Hydrolases, Plants, Toxic, Pyrophosphatases, RNA, Messenger, RNA, Viral, Rabbits, Structure-Activity Relationship, Tobacco, enzymology, Tobacco Mosaic Virus, Viral Proteins

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          Abstract

          The 7-methylguanylic acid residue confronting the 5'-terminal nucleotide of mRNA through two pyrophosphate linkages was completely removed by tobacco pyrophosphatase from mRNAs of cytoplasmic polyhedrosis virus, tobacco mosaic virus (viral RNA), and globin without any scission in the inner part of the RNA chain. Protein synthesis ability in a wheat germ cell-free system was lost after this treatment of all three kinds of mRNA. The initiation complexes for protein synthesis of these three RNAs were not obtained after using tobacco phosphodiesterase-treated mRNA. On incubation of mRNA in a wheat germ extract, the mRNA lacking m7G was quickly degraded from the 5' terminus in an exonucleolytic way, whereas the intact mRNA remained stable. These results show that one of the confronting nucleotide structure's functions is to stabilize the mRNA, to prevent its degradation.

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