Thiazole-containing peptide antibiotic. Inhibits protein synthesis by preventing binding of GTP to the 50S ribosomal subunit. Inhibits binding of elongation factor G (EF-G) and the dissociation of EF-G from the ribosome.
Product Details
| Formula: | C72H85N19O18S5 |
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| MW: | 1664.9 |
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| Source: | Isolated from Streptomyces azureus. |
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| CAS: | 1393-48-2 |
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| MI: | 14: 9364 |
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| RTECS: | XN6300100 |
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| Appearance: | White to off-white solid. |
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| Activity: | ≥900 U/mg |
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| Solubility: | Soluble in acetic acid, DMSO (10mg/ml) or dimethyl formamide; insoluble in water. |
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| Shipping: | Ambient Temperature |
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| Long Term Storage: | -20°C |
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| Handling: | Protect from light and moisture. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Effects of thiostrepton alone or in combination with selumetinib on triple-negative breast cancer metastasis: F.D. Korkmaz, et al.; Mol. Biol. Rep.
49, 10387 (2022),
Abstract;
In vivo assembling of bacterial ribosomal protein L11 into yeast ribosomes makes the particles sensitive to the prokaryotic specific antibiotic thiostrepton: A. Garcia-Marcos, et al.; Nucl. Acids Res.
35, 7109 (2007),
Abstract;
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Interaction of thiostrepton and elongation factor-G with the ribosomal protein L11-binding domain: W.S. Bowen, et al.; J. Biol. Chem.
280, 2934 (2005),
Abstract;
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Interactions of the N-terminal domain of ribosomal protein L11 with thiostrepton and rRNA: S.L. Bausch, et al.; J. Biol. Chem.
280, 29956 (2005),
Abstract;
Full Text
Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome: M.V. Rodnina, et al.; PNAS
96, 9586 (1999),
Abstract;
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The antibiotics micrococcin and thiostrepton interact directly with 23S rRNA nucleotides 1067A and 1095A: G. Rosendahl & S. Douthwaite; Nucl. Acids Res.
22, 357 (1994),
Abstract;
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Characterization of an 8.7-kilobase thiostrepton resistance-encoding plasmid (pGIF3) of Streptomyces incarnatus: H. Malina & M. Robert-Gero; Appl. Environ. Microbiol.
58, 895 (1992),
Abstract;
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Alpha-sarcin cleavage of ribosomal RNA is inhibited by the binding of elongation factor G or thiostrepton to the ribosome: S.P. Miller & J.W. Bodley; Nucl. Acids Res.
19, 1657 (1991),
Abstract;
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Recognition of the highly conserved GTPase center of 23 S ribosomal RNA by ribosomal protein L11 and the antibiotic thiostrepton: P.C. Ryan, et al.; J. Mol. Biol.
221, 1257 (1991),
Abstract;
Similarities and differences in the inhibition patterns of thiostrepton and viomycin: evidence for two functionally different populations of P sites when occupied with AcPhe-tRNA: U.R. Kutay, et al.; Biochim. Biophys. Acta
1050, 193 (1990),
Abstract;
Studies on translocation. VI. Thiostrepton prevents the formation of a ribosome-G factor-guanine nucleotide complex: J.W. Bodley, et al.; BBRC
41, 1406 (1970),
Abstract;
