Isolation of two interferon-induced translational inhibitors: a protein kinase and an oligo-isoadenylate synthetase.
Isolation of two interferon-induced translational inhibitors: a protein kinase and an oligo-isoadenylate synthetase.
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分离两种干扰素诱导的翻译抑制剂：蛋白激酶和寡聚异腺苷酸合成酶。
DOI：
10.1073/pnas.75.10.4734
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发表时间：
1978
影响因子：
11.1
通讯作者：
M. Revel
中科院分区：
文献类型：
--
作者：
A. Zilberstein;A. Kimchi;A. Schmidt;M. Revel
大规模纯化干扰素处理的小鼠L细胞中存在的翻译抑制剂，而不是在未经处理的细胞中，导致两个干扰素诱导的活动的分离。一个是蛋白激酶系统，可被双链RNA和ATP激活，并磷酸化Mr 67，000蛋白和真核起始因子-2的最小亚基。纯化的蛋白激酶是一种强的翻译抑制剂。第二种活性是一种酶，它与双链RNA一起缓慢地将ATP聚合成具有2 '-5'磷酸二酯键的寡腺苷酸。寡聚异腺苷酸反过来激活mRNA翻译的有效抑制剂。
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.