Abstract
The antibiotics, thiostrepton, siomycin, thiopeptin and sporangiomycin, are grouped here since they are similar compounds and appear to share a common mode of action. Thus, to date, these compounds have not been distinguished one from another in any assay of their modes of action nor have any bacterial mutant strains been shown to be resistant to one, but not all, members of the group. However, since these are not identical compounds, it remains possible that, in time, this grouping may become redundant; also it remains to be seen whether other compounds could be included.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Ballesta, J.P.G., Vazquez, D.: Elongation factor T-dependent hydrolysis of guanosine triphosphate resistant to thiostrepton. Proc. Natl. Acad. Sci. USA 69, 3058–3062 (1972 a)
Ballesta, J.P.G., Vazquez, D.: Reconstitution of the 50S ribosome subunit. Role of proteins L7 and L12 in the GTPase activities. Site of action of thiostrepton. FEBS Lett. 28, 337–342 (1972 b)
Bazzicalupo, M., Parisi, B., Pirali, G., Polsinelli, M., Sala, F.: Genetic and biochemical characterization of a ribosomal mutant of Bacillus subtilis resistant to sporangiomycin. Antimicrob. Agents Chemother. 8, 651–656 (1975)
Bernabeu, C., Vazquez, D., Ballesta, J.P.G.: Activities of protein-deficient particles derived from 50S ribosomal subunits by NH4Cl/Ethanol treatment. Eur. J. Biochem. 69, 233–241 (1976)
Bodley, J.W., Lin, L., Highland, J.H.: Studies on translocation VI: Thiostrepton prevents the formation of a ribosome — G factor-guanine nucleotide complex. Biochem. Biophys. Res. Commun. 41, 1406–1411 (1970 a)
Bodley, J.W., Zieve, F.J., Lin, L., Zieve, S.T.: Studies on translocation III: Conditions necessary for the formation and detection of a stable ribosome — G factor — guanosine diphosphate complex in the presence of fusidic acid. J. Biol. Chem. 245, 5656–5661 (1970 b)
Brot, N., Yamasaki, E., Redfield, B., Weissbach, H.: The properties of an E. coli ribosomal protein required for the function of factor G. Arch. Biochem. Biophys. 148, 148–155 (1972)
Brot, N., Tate, W.P., Caskey, C.T., Weissbach, H.: The requirement for ribosomal proteins L7 and L12 in polypeptide chain termination. Proc. Natl. Acad. Sci. USA 71, 89–92 (1974)
Cabrer, B., Vazquez, D., Modelell, J.: Inhibition by elongation factor G of aminoacyl-tRNA binding to ribosomes. Proc. Natl. Acad. Sci. USA 69, 733–736 (1972)
Cannon, M., Burns, K.: Modes of action of erythromycin and thiostrepton as inhibitors of protein synthesis. FEBS Lett. 18, 1–5 (1971)
Celma, M.L., Vazquez, D., Modolell, J.: Failure of fusidic acid and siomycin to block ribosomes in the pretranslocated state. Biochem. Biophys. Res. Commun. 48, 1240–1246 (1972)
Cundliffe, E.: The mode of action of thiostrepton in vivo. Biochem. Biophys. Res. Commun. 44, 912–917 (1971)
Cundliffe, E.: Antibiotic inhibitors of ribosome function. In: Molecular basis of antibiotic action. Gale, E.F., Cundliffe, E., Reynolds, P.E., Richmond, M.H., Waring, M.J. (eds.), pp. 278–379. John Wiley and Sons 1972 a
Cundliffe, E.: The mode of action of fusidic acid. Biochem. Biophys. Res. Commun. 46, 1974–1801 (1972 b)
Cundliffe, E., Dixon, P.D.: Inhibition of ribosomal A site functions by sporangiomycin and micrococcin. Antimicrob. Agents Chemother. 8, 1–4 (1975)
Cundliffe, E., Beven, J.E., Dixon, P.D.: Ribosomal effects of thiostrepton and related antibiotics. In: Topics in infectious diseases. Drews, T., Hahn, F.E. (eds.), Vol. I, pp. 167–177. Berlin-Heidelberg-New York: Springer 1975
Dixon, P.D.: Ph.D. dissertation, Univ. of Cambridge (1976)
Dixon, P.D., Beven, J.E., Cundliffe, E.: Properties of the ribosomes of antibiotic producers: Effects of thiostrepton and micrococcin on the organisms which produce them. Antimicrob. Agents Chemother. 7, 850–855 (1975)
Gaunt-Klöpfer, M., Erdmann, V.A.: ATPase and GTPase activities associated with the 5S RNA-protein complex of E. coli ribosomes. Biochim. Biophys. Acta. 390, 226–230 (1975)
Goldthwaite, C., Smith, I.: Physiological characterization of antibiotic-resistant mutants of Bacillus subtilis. Mol. Gen. Genet. 114, 190–204 (1972)
Goldthwaite, C., Dubnau, D., Smith, I.: Genetic mapping of antibiotic resistance markers in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 65, 96–103 (1970)
Hamel, E., Koka, M., Nakamoto, T.: Requirement of an E. coli 50S ribosomal protein component for effective interaction of the ribosome with T and G factors and with guanosine triphosphate. J. Biol. Chem. 247, 805–814 (1972)
Harford, N., Sueoka, N.: Chromosomal location of antibiotic resistance markers in Bacillus subtilis. J. Mol. Biol. 51, 267–286 (1970)
Highland, J.H., Lin, L., Bodley, J.W.: Studies on translocation VIII: Protection of ribosomes from thiostrepton inactivation by the binding of G factor and GDP. Biochemistry 10, 4404–4409 (1971)
Highland, J.H., Howard, G.A., Gordon, J.: Binding of thiostrepton to the ribosomes of E. coli: Characterization and stoichiometry of binding. Eur. J. Biochem. 53, 313–318 (1975 a)
Highland, J.H., Howard, G.A., Ochsner, E., Stöffler, G., Hasenbank, R., Gordon, J.: Identification of a ribosomal protein necessary for thiostrepton binding to E. coli ribosomes. J. Biol. Chem. 250, 1141–1145 (1975 b)
Hörne, J.R., Erdmann, V.A.: Effects of ethanol, methanol and different anbibiotics on the ATPase and GTPase activities associated with B. stearothermophilus 5S RNA-protein complexes. FEBS Lett. 42, 42–45 (1974)
Kinoshita, T., Liou, Y-F., Tanaka, N.: Inhibition by thiopeptin of ribosomal functions associated with T and G factors. Biochem. Biophys. Res. Commun. 44, 859–963 (1971)
Kischa, K., Möller, W., Stöffler, G.: Reconstitution of a GTPase activity by a 50S ribosomal protein from E. coli. Nature New Biol. 233, 62–63 (1971)
Liou, Y-F., Kinoshita, T., Tanaka, N., Yoshikawa, M.: Studies on the ribosomes of a thiopeptin-resistant mutant of E. coli. J. Antibiot. 26, 711–716 (1973)
Liou, Y-F., Yoshikawa, M., Tanaka, N.: Alteration of ribosomal protein L5 in a thiopeptin-resistant mutant of E. coli. Biochem. Biophys. Res. Commun. 65, 1096–1101 (1975)
Lockwood, A.H., Sarkar, P., Maitra, U., Brot, N., Weissbach, H.: Effects of thiostrepton on polypeptide chain initiation in E. coli. J. Biol. Chem. 249, 5831–5834 (1974)
Miller, D.L.: Elongation factors EF-Tu and EF-G interact at related sites on ribosomes. Proc. Natl. Acad. Sci. USA 69, 752–755 (1972)
Modolell, J., Vazquez, D., Monro, R.E.: Ribosomes, G factor and siomycin. Nature New Biol. 230, 109–112 (1971 a)
Modolell, J., Cabrer, B., Parmeggiani, A., Vazquez, D.: Inhibition by siomycin and thiostrepton of both aminoacyl-tRNA and factor G binding to ribosomes. Proc. Natl. Acad. Sci. USA 68, 1796–1800 (1971 b)
Naaktgeboren, N., Roobol, K., Gubbens, J., Voorma, H.O.: The mode of action of thiostrepton in the initiation of protein synthesis. Eur. J. Biochem. 70, 39–47 (1976)
Pestka, S.: Thiostrepton. A ribosomal inhibitor of translocation. Biochem. Biophys. Res. Commun. 40, 667–614 (1970)
Pestka, S., Bodley, J.W.: The thiostrepton group of antibiotics. In: Antibiotics. Mode of action. Corcoran, J.W., Hahn, F.E. (eds.), Vol. III, pp. 551–573. Berlin, Heidelberg, New York: Springer 1975
Pestka, S., Weiss, D., Vince, R., Wienen, B., Stöffler, G., Smith, I.: Thiostrepton — resistant mutants of Bacillus subtilis: Localization of resistance to the 50S subunit. Mol. Gen. Genet. 144, 235–241 (1976)
Pirali, G., Lancini, G.C., Parisi, B., Sala, F.: Interaction of sporangiomycin with the bacterial ribosome. J. Antibiot. 25, 561–568 (1972)
Richman, N., Bodley, J.W.: The sites on the 50S ribosomal subunit with which elongation factors Tu and G interact are at least partially identical. Proc. Natl. Acad. Sci. USA 69, 686–689 (1972)
Richter, D.: Inability of E. coli ribosomes to interact simultaneously with the bacterial elongation factors EF-Tu and EF-G. Biochem. Biophys. Res. Commun. 46, 1850–1856 (1972)
Sarkar, P., Stringer, E.A., Maitra, U.: Thiostrepton inhibition of initiation factor 1 activity in polypeptide chain initiation in E. coli. Proc. Natl. Acad. Sci. USA 71, 4986–4990 (1974)
Schrier, P.I., Möller, W.: The involvement of 50S ribosomal protein L11 in the EF G — dependent GTP hydrolysis of E. coli ribosomes. FEBS Lett. 54, 130–134 (1975)
Sopori, M.L., Lengyel, P.: Components of the 50S ribosomal subunit involved in GTP cleavage. Biochem. Biophys. Res. Commun. 46, 238–244 (1972)
Tanaka, K., Watanabe, S., Tamaki, M.: Mode of action of siomycin. J. Antibiot. 23, 13–19 (1970 a)
Tanaka, K., Watanabe, S., Teraoka, H., Tamaki, M.: Effect of siomycin on protein synthesizing activity of E. coli ribosomes. Biochem. Biophys. Res. Commun. 39, 1189–1193 (1970 b)
Tate, W.P., Beaudet, A.L., Caskey, C.T.: Guanine nucleotides and elongation factors, influence on interaction of release factors with ribosomes. Proc. Natl. Acad. Sci. USA 70, 2350–2352 (1973)
Tiboni, O., Ciferri, O.: Selective inhibition of the reactions catalysed by ribosome-specific transfer factors. FEBS Lett. 19, 174–179 (1971)
Vince, R., Weiss, D., Gordon, J., Howard, G., Smith, I., Pestka, S.: Binding of thiostrepton to ribosomes from thiostrepton-sensitive and -resistant Bacillus subtilis strains. Antimicrob. Agents Chemother. 9, 665–667 (1976)
Weisblum, B., Demohn, V.: Thiostrepton, an inhibitor of 50S ribosome subunit function. J. Bacteriol. 101, 1073–1074 (1970 a)
Weisblum, B., Demohn, V.: Inhibition by thiostrepton of the formation of a ribosome-bound guanine nucleotide complex. FEBS Lett. 11, 149–152 (1970 b)
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1979 Springer-Verlag Berlin · Heidelberg
About this chapter
Cite this chapter
Cundliffe, E. (1979). Thiostrepton and Related Antibiotics. 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_18
Download citation
DOI: https://doi.org/10.1007/978-3-642-46403-4_18
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-46405-8
Online ISBN: 978-3-642-46403-4
eBook Packages: Springer Book Archive