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本文引用的文献

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Translational regulation by the interferon-induced double-stranded-RNA-activated 68-kDa protein kinase.干扰素诱导的双链RNA激活的68 kDa蛋白激酶介导的翻译调控
Proc Natl Acad Sci U S A. 1993 May 15;90(10):4621-5. doi: 10.1073/pnas.90.10.4621.
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The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans.真核生物中从酵母到人类的翻译调控因子——真核起始因子2α蛋白激酶。
J Biol Chem. 1993 Apr 15;268(11):7603-6.
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Mechanism of interferon action: structure of the mouse PKR gene encoding the interferon-inducible RNA-dependent protein kinase.
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Mechanism of interferon action: evidence for intermolecular autophosphorylation and autoactivation of the interferon-induced, RNA-dependent protein kinase PKR.干扰素作用机制：干扰素诱导的RNA依赖性蛋白激酶PKR分子间自磷酸化和自激活的证据
J Virol. 1993 Dec;67(12):7695-700. doi: 10.1128/JVI.67.12.7695-7700.1993.
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Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene.通过呼肠孤病毒S4基因的表达逆转缺乏E3L的痘苗病毒的干扰素敏感表型。
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Mechanism of interferon action. Translational control and the RNA-dependent protein kinase (PKR): antagonists of PKR enhance the translational activity of mRNAs that include a 161 nucleotide region from reovirus S1 mRNA.干扰素作用机制。翻译控制与RNA依赖性蛋白激酶（PKR）：PKR的拮抗剂可增强包含呼肠孤病毒S1 mRNA中161个核苷酸区域的mRNA的翻译活性。
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Mechanism of interferon action motif I of the interferon-induced, RNA-dependent protein kinase (PKR) is sufficient to mediate RNA-binding activity.干扰素诱导的RNA依赖性蛋白激酶（PKR）的干扰素作用基序I的机制足以介导RNA结合活性。
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Further characterization of the protein kinase activity mediated by interferon in mouse and human cells.对干扰素在小鼠和人类细胞中介导的蛋白激酶活性的进一步表征。
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Mechanism of interferon action. Characterization of sites of phosphorylation in the interferon-induced phosphoprotein P1 from mouse fibroblasts: evidence for two forms of P1.干扰素作用机制。小鼠成纤维细胞中干扰素诱导的磷蛋白P1磷酸化位点的特性：P1两种形式的证据。
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Inhibition of mRNA binding to ribosomes by localized activation of dsRNA-dependent protein kinase.通过双链RNA依赖性蛋白激酶的局部激活抑制信使核糖核酸与核糖体的结合。
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干扰素作用机制：PKR（干扰素诱导的RNA依赖性蛋白激酶）分子间自磷酸化的特性

Mechanism of interferon action: characterization of the intermolecular autophosphorylation of PKR, the interferon-inducible, RNA-dependent protein kinase.

作者信息

Thomis D C, Samuel C E

机构信息

Department of Biological Sciences, University of California, Santa Barbara 93106, USA.

出版信息

J Virol. 1995 Aug;69(8):5195-8. doi: 10.1128/JVI.69.8.5195-5198.1995.

DOI:10.1128/JVI.69.8.5195-5198.1995
PMID:7541849
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC189345/
Abstract

The interferon-inducible, RNA-dependent protein kinase (PKR) is activated by autophosphorylation, a process mediated by double-stranded RNA. A catalytically deficient, histidine-tagged mutant PKR protein [His-PKR(K296R)] was used as the substrate for characterization of the intermolecular phosphorylation catalyzed by purified wild-type PKR [PKR(Wt)]. The intermolecular autophosphorylation of His-PKR(K296R) by PKR(Wt) was RNA dependent. Excess His-PKR(K296R) substrate inhibited both the auto- and the trans-phosphorylation activities of PKR(Wt). Inhibition of PKR(Wt) by His-PKR(K296R) was relieved by higher concentrations of activator double-stranded RNA. Phosphopeptide analysis revealed that the sites of intermolecular autophosphorylation in His-PKR(K296R) were very similar, if not identical, to the sites that were autophosphorylated in PKR(Wt) and suggest a multiple of four major phosphorylation sites per PKR molecule.

摘要

干扰素诱导的RNA依赖性蛋白激酶（PKR）通过自身磷酸化被激活，这一过程由双链RNA介导。一种催化缺陷的、带有组氨酸标签的突变型PKR蛋白[His-PKR(K296R)]被用作底物，以表征纯化的野生型PKR[PKR(Wt)]催化的分子间磷酸化。PKR(Wt)对His-PKR(K296R)的分子间自身磷酸化是RNA依赖性的。过量的His-PKR(K296R)底物抑制了PKR(Wt)的自身磷酸化和转磷酸化活性。更高浓度的激活剂双链RNA可解除His-PKR(K296R)对PKR(Wt)的抑制。磷酸肽分析表明，His-PKR(K296R)分子间自身磷酸化的位点与PKR(Wt)自身磷酸化的位点非常相似（如果不是完全相同的话），这表明每个PKR分子有多个四个主要磷酸化位点。