Biochem/physiol Actions

Primary TargetEF-G

General description

A thiazole-containing polypeptide antibiotic isolated from Streptomyces azureus. Inhibits bacterial protein synthesis and ribosomal GTPase activity by binding noncovalently, but virtually irreversibly, to the 23S rRNA in the GTPase center of the 50S subunit. Thiostrepton binding directly prevents binding to the ribosome of elongation factor G (EF-G), which also binds specifically to the 23S rRNA. Thiostrepton has proved useful in elucidating the molecular mechanisms of translation, particularly of ribosomal translocation. It is also used for selection, in bacteria of Streptomyces sp., of vectors containing the tsr gene (S. azureus), which encode a 23S rRNA methylase whose action prevents thiostrepton from binding to ribosomes.

A thiazole-containing peptide antibiotic that inhibits protein synthesis by preventing binding of GTP to 50S ribosomal subunit. Inhibits the function of elongation factor G (EF-G) and the dissociation of EF-G from the ribosome. The thiostrepton-resistant gene is also commonly used as a selective marker for recombinant DNA/plasmid technologies.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Other Notes

Rodnina, M.V., et al. 1999. Proc. Natl. Acad. Sci USA96, 9586.Rosendahl, G. and Douthwaite, S. 1994. Nucleic Acids Res.22, 357.Saarma, U. and Remme, J. 1992. Nucleic Acids Res.20, 3147.Malina, H. and Robert-Gero, M. 1992. Appl. Environ. Microbiol.58, 895.Blanco, G., et al. 1992. Gene112, 59.Miller, S.P. and Bodley, J.W. 1991. Nucleic Acids Res.19, 1657.Ryan, P.C., et al. 1991. J. Mol. Biol.221, 1257.Kutay, U.R., et al. 1990. Biochim. Biophys. Acta1050, 193.Smokvina, T., et al. 1990. Gene94, 53.Garrett, R. 1983. Trends Biochem. Sci.8, 189.Bodley, J.W., et al. 1970. Biochem. Biophys. Res. Commun.41, 1406.Thompson, J. and Cundliffe, E. 1970. Biochimie 73, 1131.

Packaging

10 g in Glass bottle

1 g in Plastic ampoule

Warning

Toxicity: Standard Handling (A)