TY - JOUR
T1 - Histone Proteins Inhibit Activation of the Interferon-Induced Protein Kinase by Binding to Double-Stranded RNA
AU - Jacobs, Bertram
AU - Imani, F.
PY - 1988/12
Y1 - 1988/12
N2 - Bulk calf thymus histone proteins, when included in reaction mixtures, inhibit activation of partially purified double-stranded (ds) RNA-dependent protein kinase, and are themselves only poorly phosphorylated. This inhibition of enzyme activation could be overcome by preincubating enzyme with dsRNA, in the absence of ATP, or by increasing the dsRNA concentration to 100 μg/ml. Under these conditions histone proteins were actively phosphorylated. In addition, histone proteins could reverse the nonactivating effects of preincubating enzyme with a high concentration of dsRNA. We demonstrate that histone proteins bind specifically to dsRNA. These results suggest that inhibition of kinase activation by histone is due to competition for binding to available dsRNA. Several virus-encoded inhibitors of the interferon-induced protein kinase are likely dsRNA-binding proteins, which may function in a manner analogous to histone proteins.
AB - Bulk calf thymus histone proteins, when included in reaction mixtures, inhibit activation of partially purified double-stranded (ds) RNA-dependent protein kinase, and are themselves only poorly phosphorylated. This inhibition of enzyme activation could be overcome by preincubating enzyme with dsRNA, in the absence of ATP, or by increasing the dsRNA concentration to 100 μg/ml. Under these conditions histone proteins were actively phosphorylated. In addition, histone proteins could reverse the nonactivating effects of preincubating enzyme with a high concentration of dsRNA. We demonstrate that histone proteins bind specifically to dsRNA. These results suggest that inhibition of kinase activation by histone is due to competition for binding to available dsRNA. Several virus-encoded inhibitors of the interferon-induced protein kinase are likely dsRNA-binding proteins, which may function in a manner analogous to histone proteins.
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U2 - 10.1089/jir.1988.8.821
DO - 10.1089/jir.1988.8.821
M3 - Article
C2 - 3230333
AN - SCOPUS:0024236043
SN - 0197-8357
VL - 8
SP - 821
EP - 830
JO - Journal of Interferon Research
JF - Journal of Interferon Research
IS - 6
ER -