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  • Title: Single-chain ribosome inactivating proteins from plants depurinate Escherichia coli 23S ribosomal RNA.
    Author: Hartley MR, Legname G, Osborn R, Chen Z, Lord JM.
    Journal: FEBS Lett; 1991 Sep 23; 290(1-2):65-8. PubMed ID: 1717316.
    Abstract:
    The rRNA N-glycosidase activities of the catalytically active A chains of the heterodimeric ribosome inactivating proteins (RIPs) ricin and abrin, the single-chain RIPs dianthin 30, dianthin 32, and the leaf and seed forms of pokeweed antiviral protein (PAP) were assayed on E. coli ribosomes. All of the single-chain RIPs were active on E. coli ribosomes as judged by the release of a 243 nucleotide fragment from the 3' end of 23S rRNA following aniline treatment of the RNA. In contrast, E. coli ribosomes were refractory to the A chains of ricin and abrin. The position of the modification of 23S rRNA by dianthin 32 was determined by primer extension and found to be A2660, which lies in a sequence that is highly conserved in all species.
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