The site of action of six different ribosome-inactivating proteins from plants on eukaryotic ribosomes: the RNA N-glycosidase activity of the proteins

Biochem Biophys Res Commun. 1988 Feb 15;150(3):1032-6. doi: 10.1016/0006-291x(88)90733-4.

Abstract

The site of action of six different ribosome-inactivating proteins from plants on eukaryotic ribosomes was studied. Treatment of ribosomes with any one of these proteins caused the 28S rRNA extracted from the inactivated ribosomes to become sensitive to treatment with aniline. A fragment containing about 450 nucleotides was released from the 28S rRNA. Further analysis of the nucleotide sequences of the 450-nucleotide fragments revealed that the aniline-sensitive phosphodiester bond was between A-4324 and G-4325 of the 28S rRNA. These results indicate that all six ribosome-inactivating proteins damage eukaryotic ribosomes by cleaving the N-glycosidic bond at A-4324 of the 28S rRNA of the ribosomes, as does ricin A-chain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aniline Compounds / pharmacology
  • Animals
  • Liver / ultrastructure
  • N-Glycosyl Hydrolases / metabolism*
  • Plant Proteins / metabolism
  • Plant Proteins / pharmacology*
  • Plants / analysis*
  • Protein Synthesis Inhibitors / metabolism
  • Protein Synthesis Inhibitors / pharmacology*
  • RNA, Ribosomal, 28S / metabolism
  • Rats
  • Ribosome Inactivating Proteins
  • Ribosomes / drug effects*

Substances

  • Aniline Compounds
  • Plant Proteins
  • Protein Synthesis Inhibitors
  • RNA, Ribosomal, 28S
  • N-Glycosyl Hydrolases
  • Ribosome Inactivating Proteins
  • aniline