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Interferon double stranded rna and protein phosphorylation characteristics of a double stranded rna activated protein kinase system partially purified from interferon treated ehrlich ascites tumor cells



Interferon double stranded rna and protein phosphorylation characteristics of a double stranded rna activated protein kinase system partially purified from interferon treated ehrlich ascites tumor cells



Journal of Biological Chemistry 253(17): 5915-5921



The addition of double-stranded RNA to an extract from mouse Ehrlich ascites tumor cells which were treated with a partially purified mouse interferon preparation promotes the phosphorylation of at least 2 proteins. The partial purification of a double-stranded RNA-activated protein kinase system from interferon-treated cells is now reported. An identically purified fraction from control cells is apparently free of the double-stranded RNA-activated protein kinase activity. The system is purified fromthe high salt wash of ribosomes from interferon-treated Ehrlich ascites tumor cells by fractional precipitation with (NH4)2 SO4 and chromatography on DEAE-cellulose and phosphocellulose. It is assayed by following the double-stranded RNA-dependent phosphorylation of histone H1 from Drosophila. The partially purified system is essentially free of double-stranded RNA-independent histone H1 kinase activity, and of (phosphorylated) histone H1 phosphatase activity. Half-maximal activation of the system is obtained at a double-stranded reovirus RNA concentration of 25 ng/ml. In activating the system poly(I) .cntdot. poly(C) can substitute for double-stranded reovirus RNA but poly(I), poly(C), poly(dI) .cntdot. poly(C), poly(I) .cntdot. poly(dC) and poly(dI) .cntdot. poly(dC) cannot. c[cyclic]AMP and cGMP do not substitute for double-stranded RNA in activating the system. A study of the kinetics of histone phosphorylation by the partially purified system indicates the existence of at least 2 phases in the process. The activation requires both double-stranded RNA and ATP but no histone. Thereafter the double-stranded RNA can be degraded (by RNase III treatment) without impairing the histone H1 phosphorylating activity.

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Accession: 005729476

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PMID: 210162



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