Abstract
Thiostrepton (alias bryamycin) is a polypeptide antibiotic of sixteen residues with several modifications to the amino acids, for example cyclizatior of cysteine residues. A portion of the molecule is cyclic and there is an ester linkage to a terminal quinaldic acid derivative (Anderson et al., 1970). Thiostrepton inhibits protein synthesis on procaryotic ribosomes by binding firmly to the 50s ribosomal subunit (Weisblum & Demohn, 1970a) with 1:1 stoichiometry (Sopori & Lengyel, 1972; Gordon & Highland, 1974) and recently (Highland et al., 1974), ribosomal protein L11 of E. coli was implicated in the thiostreptonbinding reaction. To date however, no detailed analysis of thiostreptonresistant ribosomes has been reported although a mutant of E. coli, resistant to the related antibiotic, thiopeptin, possesses altered 50s ribosomal subunits (Liou et al., 1973). Other antibiotics, chemically related to thiostrepton and thiopeptin, include siomycin and sporangiomycin, and although the complete structure is only available for thiostrepton it is already apparent that this group of compounds have identical (or closely similar) biochemical modes of action. (For a review, see Cundliffe 1972a; also Pirali et al., 1972).
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Cundliffe, E., Beven, J.E., Dixon, P.D. (1975). Ribosomal Effects of Thiostrepton and Related Antibiotics. In: Drews, J., Hahn, E. (eds) Drug Receptor Interactions in Antimicrobial Chemotherapy. Topics in Infectious Diseases, vol 1. Springer, Vienna. https://doi.org/10.1007/978-3-7091-8405-9_12
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DOI: https://doi.org/10.1007/978-3-7091-8405-9_12
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