Some ribosome-inactivating proteins depurinate ribosomal RNA at multiple sites

Biochem J. 1992 Aug 15;286 ( Pt 1)(Pt 1):1-4. doi: 10.1042/bj2860001.

Abstract

Saporin-S6, a ribosome-inactivating protein (RIP) from Saponaria officinalis released more than 1 mol of adenine/mol of ribosomes from house fly (Musca domestica) larvae and from rat liver. The release of adenine from rat liver ribosomes by several RIPs (plant enzymes with RNA N-glycosidase activity) was examined. Saporins, pokeweed antiviral protein from roots of Phytolacca americana (PAP-R), and trichokirin from Trichosanthes kirilowii seeds depurinated rat liver ribosomes at more than one site. Up to 33 mol of adenine were released from 1 mol of ribosomes. This property is not common to all RIPS.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antineoplastic Agents, Phytogenic / pharmacology*
  • Dose-Response Relationship, Drug
  • Houseflies
  • Immunotoxins*
  • Kinetics
  • Larva
  • Liver / metabolism
  • N-Glycosyl Hydrolases*
  • Plant Proteins / isolation & purification
  • Plant Proteins / pharmacology*
  • RNA, Ribosomal / metabolism*
  • Rats
  • Ribosome Inactivating Proteins, Type 1
  • Ribosomes / drug effects
  • Ribosomes / metabolism*
  • Saporins

Substances

  • Antineoplastic Agents, Phytogenic
  • Immunotoxins
  • Plant Proteins
  • RNA, Ribosomal
  • Ribosome Inactivating Proteins, Type 1
  • N-Glycosyl Hydrolases
  • Saporins