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. 1978 Oct;75(10):4734-8.
doi: 10.1073/pnas.75.10.4734.

Isolation of two interferon-induced translational inhibitors: a protein kinase and an oligo-isoadenylate synthetase

A Zilberstein, A Kimchi, A Schmidt, M Revel

Isolation of two interferon-induced translational inhibitors: a protein kinase and an oligo-isoadenylate synthetase

A Zilberstein et al. Proc Natl Acad Sci U S A. 1978 Oct.

Abstract

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.

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References

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