Interferon action: two distinct pathways for inhibition of protein synthesis by double-stranded RNA.

Abstract
Double-stranded RNA inhibits protein synthesis in at least 2 ways. It activates a protein kinase that blocks peptide chain initiation by phosphorylating the peptide chain initiation factor eIF-2 and also activates an endonuclease that inactivates different mRNA at different rates. The protein kinase and the endonuclease were partially purified from interferon-treated [mouse] Ehrlich ascites tumor cells. The 2'',5''-oligoadenylates [pppA(2''p5''A)n], found earlier to be mediators in the activation of the endonuclease by double-stranded RNA, are not mediators in the activation of the protein kinase by double-stranded RNA. [These findings have relevance to the mechanism of the antiviral effect of interferon.].

This publication has 28 references indexed in Scilit: