Proceedings of the National Academy of Sciences · 1979 · 185 citations · 32 references
C-c-a TerminusMrna TranslationMolecular BiologyAmino Acid AcceptanceInterferon TreatmentInterferon-induced Phosphodiesterase DegradingProtein SynthesisProtein ExpressionAntisense TherapyCell SignalingBiochemistryOligonucleotideGene ExpressionProtein PhosphorylationProtein BiosynthesisSignal TransductionNatural SciencesCellular BiochemistryMedicine
A phosphodiesterase characterized by a generally higher activity on 2'-5' than on 3'-5' phosphodiester bonds was isolated from mouse L cells treated with interferon. A similar enzyme was purified from mouse reticulocytes. The phosphodiesterase 2'-PDi splits the 2'-phosphate bond of pppA2'p5'A2'p5'A, the oligonucleotide activator of ribonuclease F. The level of phosphodiesterase 2'-PDi is increased by interferon treatment of L cells. The phosphodiesterase was also shown to degrade the C-C-A terminus of tRNA and to reduce the amino acid acceptance of tRNA in cell-free extracts, thereby causing a tRNA-reversible inhibition of mRNA translation.
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