CpA containing oligoribonucleotides specifically inhibit protein synthesis in rabbit reticulocytes

The diribonucleoside monophosphate CpA (and no others) inhibits polypeptide chain elongation in rabbit reticulocyte lysates at 10-50 microM. Furthermore, all the trinucleotides containing CpA, i.e., XpCpA and CpApX (X = U, C, A or G) block polypeptide chain elongation as well. At 10 microM the inhibition by XpCpA and not CpApX is transient because a 3'-exonucleolytic activity destroys the critical CpA moiety. The inhibitors do not appear to interfere with the aminoacylation of tRNAs or disrupt the interaction of amino-acyl-tRNAs with the protein synthetic machinery. High levels (200 microM) of CpA or the trinucleotides containing CpA have no effect on translation in a wheat germ cell-free system.