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Part of the book series: Antibiotics ((1512,volume 5 / 1))

Abstract

Sparsomycin, a sulfur-containing antibiotic of known structure (Wiley and Mac Kellar, 1970, 1976; Fig. 1) produced in the fermentation broth of Streptomyces sparsogenes (Argoudelis and Herr, 1962), is a potent inhibitor of the growth of many organisms, including bacteria, mammalian cells, yeasts, and molds (Owen etal., 1962; see Antibiotics I for review of earlier studies). It is thought to be identical with almarcetin, an amino acid containing antibiotic produced by a subspecies of Streptomyces albus (Bachler et al., 1964). Sparsomycin inhibits protein synthesis in Escherichia coli (Slechta, 1965) and L-cells (Goldberg and Mitsugi, 1966) while RNA synthesis continues. Sparsomycin is a highly effective inhibitor of polypeptide synthesis by ribosomes and extracts of E. coli (Goldberg and Mitsugi, 1966) and rabbit reticulocytes (Colombo et al., 1966) and by mammalian and yeast mitochondrial ribosomes (Ibrahim et al., 1974). Inhibition is exerted at a stage beyond the formation of aminoacyltRNA and its association with the ribosome by codon-anticodon interaction to form the complex active in protein synthesis (Goldberg and Mitsugi, 1966, 1967b; Hill, 1969; Ono et al., 1970). Polypeptide synthesis promoted by various synthetic polynucleotides is blocked by the antibiotic at levels below 10−7 M, the degree of inhibition being related to the base composition of the synthetic mRNA (Goldberg and Mitsugi, 1966, 1967 a). The sensitivity of polypeptide formation to sparsomycin increases markedly upon inclusion of cytidylate or guanylate in a uridylate-containing synthetic copolymer. The basis for this effect is not known.

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© 1979 Springer-Verlag Berlin · Heidelberg

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Goldberg, I.H. (1979). Sparsomycin. In: Hahn, F.E. (eds) Mechanism of Action of Antibacterial Agents. Antibiotics, vol 5 / 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-46403-4_15

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  • DOI: https://doi.org/10.1007/978-3-642-46403-4_15

  • Publisher Name: Springer, Berlin, Heidelberg

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