MOLECULAR-CLONING AND CHARACTERIZATION OF THE HUMAN DOUBLE-STRANDED-RNA ACTIVATED PROTEIN-KINASE INDUCED BY INTERFERON
MOLECULAR-CLONING AND CHARACTERIZATION OF THE HUMAN DOUBLE-STRANDED-RNA ACTIVATED PROTEIN-KINASE INDUCED BY INTERFERON
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DOI：
10.1016/0092-8674(90)90374-n
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发表时间：
1990-07-27
期刊：
影响因子：
64.5
通讯作者：
HOVANESSIAN, AG
中科院分区：
文献类型：
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作者：
MEURS, E;CHONG, K;HOVANESSIAN, AG
来自人细胞的双链（ds）RNA激活的蛋白激酶是由干扰素诱导的68 kd蛋白（p68激酶）。当在ATP存在下被dsRNA激活时，激酶变成自磷酸化的并且可以催化α-磷酸化。eIF 2的亚基，其导致蛋白质合成起始的抑制。在这里，我们报告的分子克隆和鉴定的几个相关的cDNA，从其中可以推断全长p68激酶序列。所有的cDNA都鉴定出一个2.5kb的RNA，该RNA被干扰素强烈诱导。p68激酶的推导的氨基酸序列预测了550个氨基酸的蛋白质，其含有蛋白激酶家族成员特异性的所有保守结构域，包括丝氨酸/苏氨酸激酶的催化结构域特征。在体外翻译的重建全长p68激酶cDNA产生的蛋白质的68 kd的结合dsRNA，是识别的单克隆抗体提出的对天然p68激酶，并自磷酸化。
The double-stranded (ds) RNA-activated protein kinase from human cells is a 68 kd protein (p68 kinase) induced by interferon. On activation by dsRNA in the presence of ATP, the kinase becomes autophosphorylated and can catalyze the phosphorylation of the .alpha. subunit of eIF2, which leads to an inhibition of the initiation of protein synthesis. Here we report the molecular cloning and characterization of several related cDNAs from which can be deduced the full-length p68 kinase sequence. All of the cDNAs identify a 2.5 kb RNA that is strongly induced by interferon. The deduced amino acid sequence of the p68 kinase predicts a protein of 550 amino acids containing all of the conserved domains specific for members of the protein kinase family, including the catalytic domain characteristic of serine/threonine kinases. In vitro translation of a reconstructed full-length p68 kinase cDNA yields a protein of 68 kd that binds dsRNA, is recognized by a monoclonal antibody raised against the native p68 kinase, and is autophosphorylated.