Inhibition by ricin of protein synthesis in vitro. Inhibition of the binding of elongation factor 2 and of adenosine diphosphate-ribosylated elongation factor 2 to ribosomes

Biochem J. 1975 Jan;146(1):127-31. doi: 10.1042/bj1460127.

Abstract

The binding of EF2 (elongation factor 2) and of ADP-ribosyl-EF 2 to rat liver ribosomes is inhibited by ricin. This result suggests that the native enzyme and its ADP-ribose derivative have the same or closely related binding sites on the ribosome. The inhibition by ricin of the binding of EF 2 to ribosomes is consistent with the previous observation that ricin affects EF 2-catalysed translocation during polypeptide chain elongation.

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Animals
  • In Vitro Techniques
  • Liver / drug effects
  • Molecular Weight
  • NAD / metabolism
  • Peptide Elongation Factors / antagonists & inhibitors*
  • Plant Proteins / pharmacology*
  • Protein Binding
  • Protein Biosynthesis*
  • Rats
  • Ribose / metabolism
  • Ribosomes / drug effects*
  • Ribosomes / metabolism
  • Ricin / pharmacology*

Substances

  • Peptide Elongation Factors
  • Plant Proteins
  • NAD
  • Adenosine Diphosphate
  • Ribose
  • Ricin