Isolation of two interferon-induced translational inhibitors: a protein kinase and an oligo-isoadenylate synthetase.
Large-scale purification of translational inhibitors present in interferon-treated mouse L cells, but not in untreated cells, led to the isolation of two interferon-induced activities. One is a protein kinase system that is activatable by double-stranded RNA and ATP and that phosphorylates a Mr 67,000 protein and the smallest subunit of eukaryotic initiation factor-2. The purified protein kinase is a strong translational inhibitor. The second activity is an enzyme that, with double-stranded RNA, slowly polymerizes ATP into oligoadenylate with a 2'-5' phosphodiester linkage. The oligo-isoadenylate in turn activates a potent inhibitor of mRNA translation.
D004790:Enzyme Induction; D007372:Interferons / Q000494:pharmacology*; D007739:L Cells; D009713:Nucleotidyltransferases / Q000302:isolation & purification*; D010448:Peptide Initiation Factors / Q000037:antagonists & inhibitors; D014176:Protein Biosynthesis / Q000187:drug effects*; D011494:Protein Kinases / Q000302:isolation & purification*
D010448:Peptide Initiation Factors; D007372:Interferons; D011494:Protein Kinases; D009713:Nucleotidyltransferases