Single-chain ribosome inactivating proteins from plants depurinate Escherichia coli 23S ribosomal RNA

FEBS Lett. 1991 Sep 23;290(1-2):65-8. doi: 10.1016/0014-5793(91)81227-y.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Abrin / chemistry
  • Amino Acid Sequence
  • Apurinic Acid / chemistry
  • Base Sequence
  • Binding Sites
  • Escherichia coli / ultrastructure
  • Molecular Sequence Data
  • N-Glycosyl Hydrolases*
  • Plant Proteins / pharmacology*
  • Protein Synthesis Inhibitors / pharmacology*
  • RNA, Bacterial / chemistry
  • RNA, Ribosomal / chemistry
  • RNA, Ribosomal, 23S / chemistry*
  • Ribosome Inactivating Proteins, Type 1
  • Ricin / chemistry
  • Structure-Activity Relationship


  • Plant Proteins
  • Protein Synthesis Inhibitors
  • RNA, Bacterial
  • RNA, Ribosomal
  • RNA, Ribosomal, 23S
  • RNA, ribosomal, 26S
  • Ribosome Inactivating Proteins, Type 1
  • Apurinic Acid
  • Abrin
  • Ricin
  • N-Glycosyl Hydrolases
  • MAP protein, Mirabilis jalapa
  • pokeweed antiviral protein