Fusidic acid-dependent ribosomal complexes protect Escherichia coli ribosomes from the action of the type 1 ribosome-inactivating protein crotin 2

FEBS Lett. 1993 Mar 1;318(2):189-92. doi: 10.1016/0014-5793(93)80019-q.

Abstract

The type 1 ribosome-inactivating protein crotin 2 depurinated Escherichia coli ribosomes which, upon treatment of the isolated rRNA with acid aniline, released a fragment of around 240 nucleotides whose 5'-end sequence was 5'-GAGGACCGGAGUGGAC-3'. The formation of fusidic acid-dependent ribosomal complexes completely prevented release of the fragment. Ribosomes from crotin 2-pretreated fusidic acid complexes were insensitive to acid aniline. They released the RNA fragment only after a second treatment with crotin 2 and acid aniline whereas unprotected ribosomes released the fragment directly after acid aniline.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apurinic Acid / metabolism
  • Base Sequence
  • Escherichia coli
  • Fusidic Acid / pharmacology*
  • Molecular Sequence Data
  • N-Glycosyl Hydrolases / metabolism*
  • Plant Proteins / pharmacology*
  • Protein Biosynthesis / drug effects
  • Protein Synthesis Inhibitors / pharmacology*
  • RNA, Bacterial / chemistry
  • RNA, Fungal / chemistry
  • RNA, Ribosomal / chemistry*
  • RNA, Ribosomal / drug effects
  • Ribosome Inactivating Proteins
  • Ribosome Inactivating Proteins, Type 1
  • Ribosomes / drug effects*

Substances

  • Plant Proteins
  • Protein Synthesis Inhibitors
  • RNA, Bacterial
  • RNA, Fungal
  • RNA, Ribosomal
  • Ribosome Inactivating Proteins, Type 1
  • Apurinic Acid
  • Fusidic Acid
  • N-Glycosyl Hydrolases
  • Ribosome Inactivating Proteins