Mechanism of interferon action. The interferon-induced phosphoprotein P1 possesses a double-stranded RNA-dependent ATP-binding site.
Protein P1, the interferon-induced protein phosphorylated in the presence of dsRNA in human amnion U-cells, was covalently labeled with [alpha-32P]ATP following ultraviolet irradiation. The photoaffinity labeling of protein P1 was dependent upon double-stranded RNA. Antibody prepared against phosphorylated protein P1 immunoprecipitated the double-stranded RNA-dependent photoaffinity-labeled product. The extent of photoaffinity labeling was significantly decreased by the addition of unlabeled ATP, GTP, or AMP; adenosine had little effect on the photoaffinity labeling of protein P1. These results suggest that protein P1 possesses a site capable of binding an adenine nucleotide in a double-stranded RNA-dependent manner.
J R
JR
Bischoff
C E
CE
Samuel
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000650:Amnion / Q000187:drug effects / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002460:Cell Line; D005260:Female; D006801:Humans; D007372:Interferons / Q000494:pharmacology*; D007700:Kinetics; D009705:Nucleosides / Q000378:metabolism; D009711:Nucleotides / Q000378:metabolism; D010750:Phosphoproteins / Q000096:biosynthesis* / Q000528:radiation effects; D011247:Pregnancy; D012330:RNA, Double-Stranded / Q000378:metabolism*; D011817:Rabbits; D014466:Ultraviolet Rays
D009705:Nucleosides; D009711:Nucleotides; D010750:Phosphoproteins; D012330:RNA, Double-Stranded; D000255:Adenosine Triphosphate; D007372:Interferons