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CpA containing oligoribonucleotides specifically inhibit protein synthesis in rabbit reticulocytes
Author(s) -
Wagner Thomas,
Gross Martin,
Sigler Paul B.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81368-6
Subject(s) - aminoacylation , reticulocyte , protein biosynthesis , biochemistry , chemistry , translation (biology) , elongation factor , moiety , stereochemistry , transfer rna , rna , ribosome , messenger rna , gene
The diribonucleoside monophosphate CpA (and no others) inhibits polypeptide chain elongation in rabbit reticulocyte lysates at 10–50 μM. 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 μM 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 aminoacyl‐tRNAs with the protein synthetic machinery. High levels (200 μM) of CpA or the trinucleotides containing CpA have no effect on translation in a wheat germ cell‐free system.