Oligonucleotides complementary to the alpha-sarcin domain of 28S rRNA inhibit cell-free protein synthesis

Biochem Mol Biol Int. 1993 Dec;31(5):897-903.

Abstract

Oligodeoxynucleotides complementary to the alpha-sarcin domain of rat 28S rRNA inhibit cell-free protein synthesis. The poly(U) translation system containing Artemia salina ribosomes was more sensitive to inhibition than the system containing rat liver ribosomes. The 21-mer, which was the most effective of the 7 oligonucleotides tested, hybridized with naked 28S rRNA. Hybridization with whole ribosomes, assayed by S1 nuclease protection, occurred only at high ionic strength or with ribosomes actively engaged in protein synthesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Artemia
  • Autoradiography
  • Base Sequence
  • Cell-Free System
  • Electrophoresis, Polyacrylamide Gel
  • Endoribonucleases*
  • Fungal Proteins / chemistry
  • Fungal Proteins / pharmacology*
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Nucleic Acid Hybridization
  • Oligonucleotide Probes / chemistry
  • Oligonucleotide Probes / metabolism
  • Oligonucleotide Probes / pharmacology*
  • Poly U / genetics
  • Protein Biosynthesis* / drug effects
  • Protein Synthesis Inhibitors / chemistry
  • Protein Synthesis Inhibitors / pharmacology*
  • RNA, Ribosomal, 28S
  • Rabbits
  • Rats
  • Ribosomes / metabolism

Substances

  • Fungal Proteins
  • Oligonucleotide Probes
  • Protein Synthesis Inhibitors
  • RNA, Ribosomal, 28S
  • alpha-sarcin
  • Poly U
  • Endoribonucleases