Abstract
THE 12,13-epoxytrichothecenes (Fig. 1) form a group of fungal toxins with a tricyclic trichothecene ring system. (For review, see ref. 1). They have been shown to inhibit protein synthesis in a variety of eukaryotic systems2 and in particular they block peptidyl transferase activity as determined by the puromycin-fragment reaction3. More recent studies have shown however, that the trichothecenes have differential effects on protein synthesis in whole cells4. One subgroup containing verrucarin A and T-2 toxin inhibited initiation (I-type), and the other subgroup inhibited elongation/termination (E-type); trichodermin was in the latter group. Here I show that these two classes can also be distinguished in cell-free systems and suggest analogies with the mode of action of the lincosaminide and macrolide inhibitors of protein synthesis in prokaryotes.
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SCHINDLER, D. Two classes of inhibitors of peptidyl transferase activity in eukaryotes. Nature 249, 38–41 (1974). https://doi.org/10.1038/249038a0
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DOI: https://doi.org/10.1038/249038a0
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