Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
, 71 (1), 30-4

Mechanism of Inhibition of Eukaryotic Protein Synthesis by Trichothecene Fungal Toxins

Mechanism of Inhibition of Eukaryotic Protein Synthesis by Trichothecene Fungal Toxins

E Cundliffe et al. Proc Natl Acad Sci U S A.

Abstract

The 12,13-epoxytrichothecenes, a group of sesquiterpenoid fungal antibiotics, inhibit protein synthesis in eukaryotic cells but do not share a common mode of action. Trichodermin stabilizes polyribosomes, prevents their disaggregation by puromycin, and also prevents the release of nascent peptides from ribosomes by puromycin. Nivalenol, T-2 toxin, and verrucarin A cause rapid and almost quantitative breakdown of polyribosomes in H-HeLa cells, a process which is inhibited by anisomycin, cycloheximide, or trichodermin. Similar effects of trichodermin, nivalenol, and verrucarin A are also observed in yeast spheroplasts. We conclude that nivalenol, T-2 toxin, and verrucarin A are potent and highly selective inhibitors of polypeptide chain initiation in eukaryotes, whereas trichodermin inhibits chain elongation and (or) termination. We have compared the structural formulae of various trichothecenes and suggest that the presence of substituents on carbon-15 of the common trichothecene ring may be important in determining the precise modes of action of this group of compounds.

Similar articles

See all similar articles

Cited by 66 PubMed Central articles

See all "Cited by" articles

References

    1. Mol Pharmacol. 1967 Sep;3(5):401-11 - PubMed
    1. J Mol Biol. 1967 Nov 28;30(1):137-46 - PubMed
    1. Jpn J Med Sci Biol. 1968 Jun;21(3):185-94 - PubMed
    1. Cancer Res. 1968 Nov;28(11):2393-6 - PubMed
    1. J Biochem. 1968 Oct;64(4):479-85 - PubMed

MeSH terms

LinkOut - more resources

Feedback