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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. CpA containing oligoribonucleotides specifically inhibit protein synthesis in rabbit reticulocytes. Wagner, T., Gross, M., Sigler, P.B. FEBS Lett. (1987) [Pubmed]
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