Inhibition of protein synthesis in Saccharomyces cerevisiae by the 12,13-epoxytrichothecenes trichodermol, diacetoxyscirpenol and Verrucarin A. Reversibility of the effects.
- 1 January 1982
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 35 (7) , 875-881
- https://doi.org/10.7164/antibiotics.35.875
Abstract
Inhibition of protein synthesis by trichodermol, diacetoxyscirpenol and verrucarin A in cells and spheroplasts of S. cerevisiae was investigated. Inhibition was reversible for trichodermol and diacetoxyscirpenol, both drugs being removed from their target site(s) by washing, but was irreversible for verrucarin A. These results are interpreted in relation to variations in chemical structure between these trichothecenes.This publication has 4 references indexed in Scilit:
- Mechanism of action of the 12,13-epoxytrichothecene, anguidine, an inhibitor of protein synthesisBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1976
- Competition between trichodermin and several other sesquiterpene antibiotics for binding to their receptor site(s) on eukaryotic ribosomesBiochemical Journal, 1976
- Prevention, by ribosome-bound nascent polyphenylalanine chains, of the functional interaction of t-2 toxin with its receptor siteBiochemical Journal, 1976
- Inhibition of protein synthesis in reticulocyte lysates by trichoderminBiochemical Journal, 1976