Inhibitors of polypeptide elongation on yeast polysomes

J Antibiot (Tokyo). 1975 Jun;28(6):453-62. doi: 10.7164/antibiotics.28.453.

Abstract

Yeast polysomes are very active for amino acid incorporation when supplemented with elongation factors and the different components required for elongation of the polypeptide chain. This polysomal system is suitable for the study of the individual streps of the elongation cycle and to test the effect of different inhibitors. Anisomycin, trichodermin, trichodermol, trichothecin, fusarenon X, sparsomycin and blasticidin S inhibit peptide bond formation on these polysomes, whereas diphtheria toxin, pederine, cycloheximide and cryptopleurine block translocation.

MeSH terms

  • Amino Acids / metabolism
  • Anisomycin / pharmacology
  • Cycloheximide / pharmacology
  • Diphtheria Toxin / pharmacology
  • Peptide Chain Elongation, Translational / drug effects*
  • Polyribosomes / drug effects*
  • Polyribosomes / metabolism
  • Potassium / pharmacology
  • Puromycin / pharmacology
  • Pyrans / pharmacology
  • RNA, Transfer
  • Saccharomyces cerevisiae / drug effects*
  • Saccharomyces cerevisiae / metabolism
  • Sparsomycin / pharmacology
  • Translocation, Genetic / drug effects
  • Trichodermin / pharmacology

Substances

  • Amino Acids
  • Diphtheria Toxin
  • Pyrans
  • Trichodermin
  • Puromycin
  • Anisomycin
  • Sparsomycin
  • RNA, Transfer
  • Cycloheximide
  • Potassium