Abstract
Streptomycin was isolated from cultures of Streptomyces griseus by Waksman and his colleagues in 1944 (Schatz et al., 1944). Subsequently, numerous other aminoglycosides, with similar actions as well as structures, were discovered. All are carbohydrate molecules containing one or more glycosidic linkages and a large number of hydrophilic groups, including several amino or guanidino groups (see review by Umezawa, 1975).
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
Anand, N., Davis, B.D.: Effect of streptomycin on Escherichia coli. Nature (London) 185, 22–23 (1960)
Anand, N., Davis, B.D., Armitage, A.K.: Uptake of streptomycin by Escherichia coli. Nature 185, 23–24 (1960)
Anderson, P., Davies, J.E., Davis, B.D.: The effect of spectinomycin on polypeptide synthesis in extracts of Escherichia coli. J. Mol. Biol. 29, 203–208 (1967)
Anderson, W.F., Gorini, L., Breckenridge, L.: Role of ribosomes in streptomycin-activated suppression. Proc. Natl. Acad. Sci. USA 54, 1076–1083 (1965)
Andry, K., Bockrath, R.C.: Dihydrostreptomycin accumulation in E. coli. Nature (London) 251, 534–536 (1974)
Baan, R.A., Duijfjes, J.J., Van Leerdam, E., Van Knippenberg, P.H., Bosch, L.: Specific in situ cleavage of 16S ribosomal RNA of Escherichia coli interferes with the function of initiation factor IF-1. Proc. Natl. Acad. Sci. USA 73, 702–706 (1976)
Bayliss, F.T., Ingraham, J.L.: A mutation in S. cerevisiae conferring streptomycin and cold-sensitivity by affecting ribosome formation and function. J. Bacteriol. 118, 319–328 (1974)
Beggs, W.H., Andrews, F.A.: Inhibition of dihydrostreptomycin action on Mycobacterium smegmatis by monovalent and divalent cation salts. Antimicrob. Agents Chemother. 7, 636–639 (1975)
Beggs, W.H., Andrews, F.A.: Inhibition of dihydrostreptomycin binding to Mycobacterium smegmatis by monovalent and divalent cation salts. Antimicrob. Agents Chemother. 9, 393–396 (1976)
Benveniste, R., Yamada, T., Davies, J.: Enzymatic adenylylation of streptomycin and spectinomycin by R-factor-resistant Escherichia coli. Infect. Immun. 1, 109–119 (1970)
Berkman, S., Henry, R.J., Housewright, R.D.: Studies on streptomycin. J. Bacteriol. 53, 567–574 (1947)
Bermingham, M.A.C., Deol, B.S., Still, J.L.: Effect of streptomycin on lipid composition with particular reference to cyclic depsipeptide biosynthesis in Serratia marcescens and other microorganisms. Biochem. J. 119, 861–869 (1970)
Birge, E.A., Kurland, C.G.: Altered ribosomal protein in streptomycin-dependent Escherichia coli. Science 166, 1282–1284 (1969)
Bissel, M.D.: Formation of an altered enzyme in E. coli in the presence of neomycin. J. Mol. Biol. 14, 619–622 (1965)
Biswas, D.K., Gorini, L.: The attachment site of streptomycin to the 30S ribosomal subunit. Proc. Natl. Acad. Sci. USA 69, 2141–2144 (1972 a)
Biswas, D.K., Gorini, L.: Restriction, de-restriction and mistranslation in missense suppression. Ribosomal discrimination of tRNA’s. J. Mol. Biol. 64, 119–134 (1972 b)
Bjare, U., Gorini, L.: Drug dependence reversed by a ribosomal ambiguity mutation, ram, in Escherichia coli. J. Mol. Biol. 57, 423–435 (1971)
Blomberg, C.: A kinetic recognition process for tRNA at the ribosome. J. Theor. Biol. 66, 307–325 (1977)
Bollen, A., Davies, J., Ozaki, M., Mizushima, S.: Identification of the ribosomal protein conferring sensitivity to the antibiotic spectinomycin in Escherichia coli. Science 165, 85–86 (1969)
Brakier-Gingras, L., Provost, L., Dugas, H.: Conformational changes induced in Escherichia coli ribosomes by streptomycin. A spin label study. Biochem. Biophys. Res. Commun. 60, 1238–1244 (1974 a)
Brakier-Gingras, L., Lacoste, L., Boileau, G.: Streptomycin resistance and ribosomal proteins: Amino acid substitutions in the str protein of one streptomycin-resistant mutant of Escherichia coli K12 after mutagenesis with ethyl methanesulphonate. Can. J. Biochem. 52, 304–309 (1974 b) Branscomb, E.W., Galas, D.J.: Progressive decrease in protein synthesis accuracy induced by streptomycin in Escherichia coli. Nature (London) 254, 161–163 (1975)
Breckenridge, L., Gorini, L.: The dominance of streptomycin sensitivity re-examined. Proc. Natl. Acad. Sci. USA 62, 979–985 (1969)
Breckenridge, L., Gorini, L.: Genetic analyses of streptomycin resistance in Escherichia coli. Genetics 65, 9–25 (1970)
Breson, K., Petersen, B.N., Rasmussen, F.: Ototoxicity in 626 patients with pulmonary tuberculosis treated with dihydrostreptomycin, streptomycin sulphate, or a combination of both. Scand. J. Res. Dis. 53, 44–49 (1972)
Brock, T.D.: Streptomycin. Symp. Soc. Gen. Microb. 16, 131 (1966)
Brownstein, B.L., Lewandowski, L.J.: A mutation supressing streptomycin dependence. 1. An effect of ribosome function. J. Mol. Biol. 25, 99–109 (1967)
Bryan, L.E., Van den Elzen, H.M.: Streptomycin accumulation in susceptible and resistant strains of Escherichia coli and Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 9, 928–938 (1976)
Bryan, L.E., Van den Elzen, H.M.: Effects of membrane-energy mutations and cations on streptomycin and gentamicin accumulation by bacteria: a model for entry of streptomycin and gentamicin in susceptible and resistant bacteria. Antimicrob. Agents Chemother. 12, 163–177 (1977)
Burns, D.J.W., Cundliffe, E.: Bacterial protein synthesis: A novel system for studying antibiotic action in vivo. Eur. J. Biochem. 37, 570–574 (1973)
Butlin, J.D., Cox, G.B., Gibson, F.: Oxidative phosphorylation in Escherichia coli K12: Mutations affecting magnesium ion- or, calcium ion-stimulated adenosine triphosphatase. Biochem. J. 124, 75–81 (1971)
Butlin, J.D., Cox, G.B., Gibson, F.: Oxidative phosphorylation in Escherichia coli K12: the genetic and biochemical characterization of a strain carrying a mutation in the uncB gene. Biochim. Biophys. Acta 292, 366–375 (1973)
Cannon, M., Cabezon, T., Bollen, A.: Mapping of neamine resistance: identification of two genetic loci, neaA and neaB. Mol. Gen. Genet. 130, 321–326 (1974)
Caskey, T., Scolnick, E., Tompkins, R., Goldstein, J., Milman, G.: Peptide chain termination, codon, protein factor and ribosomal requirements. Cold Spring Harbor Symp. Quant. Biol. 34, 479–488 (1969)
Caskey, C.T., Bosch, L., Konecki, D.S.: Release factor binding to ribosome requires an intact 16S rRNA 3′ terminus. J. Biol. Chem. 252, 4435–4437 (1977)
Chakrabarti, S.L., Gorini, L.: A link between streptomycin and rifampicin mutation. Proc. Natl. Acad. Sci. USA 72, 2085–2087 (1975)
Chakrabarti, S.L., Gorini, L.: Interaction between mutations of ribosomes and RNA polymerase: A pair of str A and rif mutants individually temperature-insensitive but temperature-sensitive in combination. Proc. Natl. Acad. Sci. USA 74, 1157–1161 (1977)
Chang, F.N., Flaks, J.G.: Topography of the Escherichia coli 30S ribosomal subunit and streptomycin binding. Proc. Natl. Acad. Sci. USA 67, 1321–1328 (1970)
Chang, F.N., Flaks, J.G.: The binding of dihydrostreptomycin to E. coli ribosomes: characteristics and equilibrium of the reaction. Antimicrob. Agents Chemother. 2, 294–307 (1972 a)
Chang, F.N., Flaks, J.G.: The binding of dihydrostreptomycin to E. coli ribosomes: kinetics of the reaction. Antimicrob. Agents Chemother. 2, 308–319 (1972 b)
Chang, F.N., Wang, Y.J., Fetterolf, C.J., Flaks, J.G.: Unequal contribution to ribosomal assembly of both str alleles in Escherichia coli merodiploids and its relationship to the dominance phenomenon. J. Mol. Biol. 82, 273–277 (1973)
Cornelius, C.E., III, Domeseik, G.: Spectinomycin hydrochloride in the treatment of uncomplicated gonorrhoea. B.J. Vener. Dis. 46, 212–213 (1970)
Cox, E.C., White, J.R., Flaks, J.G.: Streptomycin action and the ribosome. Proc. Natl. Acad. USA 51, 703–709 (1964)
Dahlberg, A.E., Dahlberg, J.E.: Binding of ribosomal protein SI of Escherichia coli to the 3′ end of 16S rRNA. Proc. Natl. Acad. Sci. USA 72, 2940–2944 (1975)
Dahlberg, A.E., Lund, E., Kjeldgaard, N.O.: Some effects of antibiotics on bacterial polyribosomes as studied by gel electrophoresis. J. Mol. Biol. 78, 627–636 (1973 a)
Dahlberg, A.E., Lund, E., Kjeldgaard, N.O., Bowman, C.M., Nomura, M.: Colicin E3 induced cleavage of 16S ribosomal ribonucleic acid; blocking effects of certain antibiotics. Biochemistry 12, 948–950 (1973 b)
Davies, J.E.: Studies on the ribosomes of streptomycin-sensitive and resistant strains of Escherichia coli. Proc. Natl. Acad. Sci. USA 51, 659–664 (1964)
Davies, J.: Streptomycin and the genetic code. Cold Spring Harbor Symp. Quant. Biol. 31, 665–670 (1966)
Davies, J.E., Davis, B.D.: Misreading of RNA code words induced by aminoglycoside antibiotics: the effect of drug concentration. J. Biol. Chem. 243, 3312–3316 (1968)
Davies, J., Gilbert, W., Gorini, L.: Streptomycin, suppression and the code. Proc. Natl. Acad. Sci. USA 51, 883–890 (1964)
Davies, J., Anderson, P., Davis, B.D.: Inhibition of protein synthesis by spectinomycin. Science 149, 1096–1098 (1965 a)
Davies, J., Gorini, L., Davis, B.D.: Misreading of RNA codewords induced by aminoglycoside antibiotics. Mol. Pharmacol. 1, 93–106 (1965 b)
Davies, J.E., Jones, D.S., Khorana, J.G.: A further study of misreading of codons induced by streptomycin and neomycin using ribopolynucleotides containing two nucleotides in alternating sequence as templates. J. Mol. Biol. 18, 48–57 (1966)
Davies, B.D.: The mechanism of action of aminoglycoside antibiotics. Asian Med. J. 11, 16–23 (1968)
Davis, B.D., Tai, P-C., Wallace, B.J.: Complex interactions of antibiotics with the ribosome. In: Ribosomes. Nomura, M., Tissieres, A., Lengyel, P. (eds.), p. 771. New York: Cold Spring Harbor 1974
Delihas, N., Topol, E., Larrinua, I.: Changes in accessibility to chemical modification of Escherichia coli ribosomes induced by streptomycin. FEBS Lett. 53, 170–175 (1975)
Demain, A.L., Inamine, E.: Biochemistry and regulation of streptomycin and mannosidostreptomycinase (α-D-Mannosidase) formation. Bacteriol. Rev. 34, 1–19 (1970)
Deusser, E., Stöffler, G., Wittmann, H.G., Apirion, D.: Ribosomal proteins XVI. Altered S4 proteins in Escherichia coli revertants from streptomycin dependence to independence. Molec. Gen. Genet. 109, 298–302 (1970)
De Wilde, M., Cabezon, T., Villarroel, R., Herzog, A., Bollen, A.: Cooperative control of translational fidelity by ribosomal proteins in Escherichia coli. I. Properties of ribosomal mutants whose resistance to neamine is the cumulative effect of two distinct mutations. Mol. Gen. Genet. 142, 19–33 (1975)
Donovick, R., Bayan, A.P., Canales, P., Pancy, F.: The influence of certain substances on the activity of streptomycin. III Differential effects of various electrolytes on the action of streptomycin. J. Bacteriol. 56, 125–137 (1948) Dubin, D.T., Davis, B.D.: The effect of streptomycin on potassium flux in Escherichia coli. Biochim. Biophys. Acta 52, 400–402 (1961)
Dubin, D.T., Hancock, R., Davis, B.D.: The sequence of some effects of streptomycin in Escherichia coli. Biochim. Biophys. Acta 74, 476–489 (1963)
Duncan, W.C., Holder, W.R., Roberts, D.P., Knox, J.M.: Treatment of gonorrhoea with spectinomycin hydrochloride: comparison with penicillin schedules. Antimicrob. Agents Chemother. 1, 210–214 (1972)
Elseviers, D., Gorini, L.: In drug action and drug resistance in bacteria 2. Aminoglycoside antibiotics. Mutsuhashi, S. (ed.). University Park Press 1975
Erdös, T., Ullman, A.: Effect of streptomycin on the incorporation of amino-acids labelled with carbon-14 into ribonucleic acid and protein in a cell-free system of Mycobacterium. Nature (London) 183, 618–619 (1959)
Erdös, T., Ullman, A.: Effect of streptomycin on the incorporation of tyrosine labeled with carbon-14 into protein of Mycobacterium cell fractions in vivo. Nature (London) 185, 100–101 (1960)
Erlanson, P., Lundgren, A.: Ototoxic side effects following treatment with streptomycin. Acta Med. Scand. 176, 147–163 (1964)
Falbe-Hansen, J., Rasmussen, F., Worsoe-Petersen, J.: Ototoxic side effects of the streptomycins, particularly dihydrostreptomycin. Scand. J. Res. Dis. 53, 38–43 (1972)
Fitzgerald, R.J., Bernheim, F., Fitzgerald, D.B.: The inhibition by streptomycin of adaptive enzyme formation in Mycobacteria. J. Biol. Chem. 175, 195–200 (1948)
Flaks, J.G., Cox, E.C., Witting, M.L., White, J.R.: Polypeptide synthesis with ribosomes from streptomycin-resistant and dependent E. coli. Biochem. Biophys. Res. Commun. 7, 390–393 (1962)
Freda, C.E., Cohen, S.S.: Nature of ribonucleic acid stimulated by streptomycin in the absence of protein synthesis. J. Bacteriol. 92, 1680–1688 (1966)
Funatsu, G., Wittmann, H.G.: Ribosomal proteins XXXIII: Location of amino-acid replacements in protein S 12 isolated from Escherichia coli mutants resistant to streptomycin. J. Mol. Biol. 68, 547–550 (1972)
Galas, D.J., Branscomb E.W.: Ribosome slowed by mutation to streptomycin resistance. Nature (London) 262, 617–619 (1976)
Gale, E.F., Cundliffe, E., Reynolds, P.E., Richmond, M.H., Waring, M.J.: The molecular basis of antibiotic action, pp. 278–379. London, New York: Wiley Interscience 1972
Garcia-Patrone, M., Perazzolo, C.A., Baralle, F., Gonzalez, N.S., Algranati, I.D.: Studies on dissociation factor of bacterial ribosomes: Effect of antibiotics. Biochim. Biophys. Acta 246, 291–299 (1971)
Garvin, R.T., Rosset, R., Gorini, L.: Ribosomal assembly influenced by growth in the presence of streptomycin. Proc. Natl. Acad. Sci. USA 70, 2762–2766 (1973)
Garvin, R.T., Biswas, D.K., Gorini, L.: The effects of streptomycin or dihydrostreptomycin binding to 16S RNA or to 30S ribosomal subunits. Proc. Natl. Acad. Sci. USA 71, 3814–3818 (1974)
Gavrilova, L.P., Kostiashkina, O.E., Koteliansky, V.E., Rutkevitch, N.M., Spirin, A.S.: Factor-free (“non-enzymic”) and factor-dependent systems of translation of polyuridylic acid by Escherichia coli ribosomes. J. Mol. Biol. 101, 537–552 (1976)
Gilbert, D.N., Kutscher, E., Ireland, P., Barnett, J.A., Sanford, J.P.: Effect of concentrations of magnesium and calcium on the in vitro susceptibility of Pseudomonas aeruginosa to gentamycin. J. Infect. Dis. 124, 37–45 (1971)
Ginzburg, I., Miskin, R., Zamir, A.: N-Ethyl maleimide as a probe for the study of functional sites and conformations of 30 S ribosomal subunits. J. Mol. Biol. 79, 481–494 (1973)
Girshovich, A., Bochkareva, E.S., Ouchinnikov, Y.A.: Identification of components of the streptomycin-binding center of E. coli MRE600 ribosomes by photo-affinity labelling. Mol. Gen.. Genet. 144, 205–212 (1976)
Gorini, L.: Ribosomal discrimination of tRNAs. Nature (New Biol.) 234, 261–264 (1971)
Gorini, L.: Streptomycin and misreading of the genetic code. In: Ribosomes. Nomura, M., Tissieres, A., Lengyel, P. (eds.), pp. 791–803 Cold Spring Harbor, New York: Cold Spring Harbor Lab. 1974
Gorini, L., Kataja, E.: Phenotypic repair by streptomycin of defective genotypes in E. coli. Proc. Natl. Acad. Sci. USA 51, 487–493 (1964)
Gorini, L., Kataja, E.: Suppression activated by streptomycin and related antibiotics in drug-sensitive strains. Biochem. Biophys. Res. Commun. 18, 656–663 (1965)
Gorini, L., Rosset, R., Zimmerman, R.A.: Phenotypic masking and streptomycin dependence. Science 157, 1314–1317 (1967)
Green, S.R., Waksman, S.A.: Effect of glucose, peptone and salts on streptomycin activity. Proc. Soc. Exp. Biol. Med. 67, 281–285 (1948)
Gupta, R.S., Schlessinger, D.: Coupling of rates of transcription, translation and messenger ribonucleic acid degradation in streptomycin-dependent mutants of Escherichia coli. J. Bacteriol. 125, 84–93 (1976)
Gurgo, C., Apirion, D., Schlessinger, D.: Polysome metabolism in Escherichia coli treated with chloramphenicol, neomycin, spectinomycin or tetracycline. J. Mol. Biol. 45, 205–220 (1969)
Hancock, R.: Uptake of 14C-streptomycin by Bacillus megaterium. J. Gen. Microbiol. 28, 503–516 (1962 a)
Hancock, R.: Uptake of 14C-streptomycin by some microorganisms and its relation to their streptomycin sensitivity. J. Gen. Microbiol. 28, 493–501 (1962 b)
Harwick, H.J., Kalmanson, G.M., Guze, L.B.: In vitro activity of ampicillin or vancomycin combined with gentamicin or streptomycin against enterococci. Antimicrob. Agents Chemother. 4, 383–387 (1973)
Hasenbank, R., Guthrie, C., Stöffler, G., Wittmann, H.G., Rosen, L., Apirion, D.: Electrophoretic and immunological studies on ribosomal proteins of 100 Escherichia coli revertants from streptomycin dependence. Mol. Gen. Genet. 127, 1–18 (1973)
Heimark, R.L., Kahan, L., Johnson, K., Hershey, J.W.B., Traut, R.R.: Crosslinking of initiation factor IF 3 to proteins of the Escherichia coli 30S ribosomal subunit. J. Mol. Biol. 105, 219–230 (1976)
Held, W.A., Gette, W.R., Nomura, M.: Role of 16 S ribonucleic acid and the 30 ribosomal protein S12 in the initiation of natural messenger ribonucleic acid translation. Biochemistry 13, 2115–2122 (1974)
Herzog, A.: An effect of streptomycin on the dissociation of Escherichia coli 70S ribosomes.
Biochem. Biophys. Res. Commun. 15, 172–176 (1964)
Herzog, A., Ghysen, A., Bollen, A.: Sensitivity and resistance to streptomycin in relation with factor-mediated dissociation of ribosomes. FEBS Lett. 15, 291–294 (1971)
Hirashima, A., Kaji, A.: Purification and properties of ribosome-releasing factor. Biochemistry 11, 4037–4044 (1972)
Hirashima, A., Kaji, A.: Role of elongation factor G and a protein factor on the release of ribosomes from messenger ribonucleic acid. J. Biol. Chem. 248, 7580–7587 (1973)
Hopfield, J.J.: Kinetic proofreading: A new mechanism for reducing errors in biosynthetic processes requiring high specificity. Proc. Natl. Acad. Sci. USA 71, 4135–4139 (1974)
Hurwitz, C., Rosano, C.L.: Accumulation of label from 14C-streptomycin by Escherichia coli. J. Bacteriol. 83, 1193–1201 (1962)
Igarashi, K., Ishitsuka, H., Kaji, A.: Comparative studies on the mechanism of action of lincomycin, streptomycin, and erythromycin. Biochem. Biophys. Res. Commun. 37, 499–504 (1969)
Iida, K., Koike, M.: Cell wall alterations of Gram-negative bacteria by aminoglycoside antibiotics. Antimicrob. Agents Chemother. 5 (1), 95–97 (1974)
Kaji, H., Kaji, A.: Specific binding of sRNA to ribosomes: Effect of streptomycin. Proc. Natl. Acad. Sci. USA 54, 213–219 (1965)
Kaji, H., Tanaka, Y.: Binding of dihydrostreptomycin to ribosomal subunits. J. Mol. Biol. 32, 221–230 (1968)
Kaji, H., Suzuka, I., Kaji, A.: Binding of specific soluble ribonucleic acid to ribosomes: Binding of soluble ribonucleic acid to the template-30S subunits complex. J. Biol. Chem. 241, 1251–1256 (1966)
Kang, S.-S.: A mutant of Escherichia coli with temperature-sensitive streptomycin protein. Proc. Natl. Acad. Sci. USA 65, 544–550 (1970 a)
Kang, S.-S.: Temperature sensitivity alteration of 30S subunits demonstrated by in vitro reassociation of functional ribosomes. Nature (London) 225, 1132–1133 (1970 b)
Karney, W., Holmes, K.K., Turck, M.: Comparison of five aminocyclitol antibiotics in vitro against enterobacteriaceae and Pseudomonae. Antimicrob. Agents Chemother. 3, 338–342 (1973)
Kawabe, H., Mitsuhashi, S.: Inactivation of dihydrostreptomycin by Staphylococcus aureus. Jpn. J. Microbiol. 15, 545–548 (1971)
Kogut, M., Harris, M.: Effect of streptomycin in bacterial cultures growing at different rates; interaction with bacterial ribosomes in vivo. Eur. J. Biochem. 9, 42–49 (1969)
Kogut, M., Prizant, E.: Effects of dihydrostreptomycin treatment in vivo on the ribosome cycle in Escherichia coli. FEBS Lett. 12, 17–20 (1970)
Kogut, M., Lightbown, J.W., Isaacson, P.: Streptomycin action and anaerobiosis. J. Gen. Microbiol. 39, 155–164 (1965)
Kogut, M., Maltby, E.N., Prizant, E.: Effects of dihydrostreptomycin on bacterial ribosomes in vivo. Biochem. J. 119, 121–123 (1970)
Kreider, G., Brownstein, B.L.: A mutation suppressing streptomycin dependence, II. An altered protein in the 30S ribosomal subunit. J. Mol. Biol. 61, 135–142 (1971)
Kreider, G., Brownstein, B.L.: Ribosomal proteins involved in the suppression of streptomycin dependence in Escherichia coli. J. Bacteriol. 109, 780–785 (1972)
Kreider, G., Brownstein, B.: Pleiotropic effects resulting from mutations in genes for ribosomal proteins: Analysis of revertants from streptomycin dependence. J. Mol. Biol. 84, 159–171 (1974)
Kung, H.-F., Treadwell, B., Spears, C., Tai, P.-C, Weissbach, H.: DNA-directed synthesis in vitro for β-galactosidase: requirement for a ribosome release factor. Proc. Natl. Acad. Sci. USA 74, 3217–3221 (1977)
Kurland, C.G.: Structure and function of the bacterial ribosome. Annu. Rev. Biochem. 46, 173–200 (1977)
Kurland, C.G., Rigler, R., Ehrenberg, M., Blomberg, C.: Allosteric mechanism for codon-dependent tRNA selection on ribosomes. Proc. Natl. Acad. Sci. USA 72, 4248–4251 (1975)
Lake, J.A.: Ribosome structure determined by electron microscopy of Escherichia coli small subunits, large subunits and monomeric ribosomes. J. Mol. Biol. 105, 131–159 (1976)
Lake, J.A.: Aminoacyl-tRNA binding at the recognition site is the first step of the elongation cycle of protein synthesis. Proc. Natl. Acad. Sci. USA 74, 1903–1907 (1977)
Lederberg, E.M., Cavalli-Sforza, L., Lederberg, J.: Interaction of streptomycin and a suppressor for galactose fermentation in E. coli K 12. Proc. Natl. Acad. Sci. USA 51, 678–682 (1964)
Lederberg, J.: Streptomycin-resistance: A genetically recessive mutation. J. Bacteriol. 61, 549–550 (1951)
Lelong, J.C., Cousin, M.A., Gros, D., Grunberg-Manago, M., Gros, F.: Streptomycin induced release of fMet-tRNA from the ribosomal initiation complex. Biochem. Biophys. Res. Commun. 42, 530–537 (1971)
Lelong, J.C., Cousin, M.A., Miskin, R., Vogel, Z., Groner, Y., Revel, M.: Protection of Escherichia coli ribosomes against streptomycin by purified initiation factors. Eur. J. Biochem. 27, 174–180 (1972)
Lelong, J.C., Gros, D., Gros, F., Bollen, A., Maschler, R., Stöffler, G.: Function of individual 30 S subunit proteins of Escherichia coli. Effect of specific immunoglobulin fragments (Fab) on activities of ribosomal decoding sites. Proc. Natl. Acad. Sci. USA 71, 248–252 (1974)
Lemieux, R.U., Wolfrom, M.L.: The chemistry of streptomycin. Adv. Carbohyd. Chem. 3, 337–384 (1948)
Lennette, E., Apirion, D.: The level of fMet-tRNA on ribosomes from streptomycin treated cells. Biochem. Biophys. Res. Commun. 41, 804–811 (1970)
Leon, S.A., Brock, T.D.: Effect of streptomycin and neomycin on physical properties of the ribosome. J. Mol. Biol. 24, 391–404 (1967)
Levanen, J., Nordman, R.: Complete respiratory paralysis caused by a large dose of streptomycin and its treatment with calcium chloride. Ann. Clin. Res. 7, 47–49 (1975)
Likover, T.E., Kurland, C.G.: Ribosomes from a streptomycin-dependent strain of Escherichia coli. J. Mol. Biol. 25, 497–504 (1967 a)
Likover, T.E., Kurland, C.G.: The contribution of DNA to translation errors induced by streptomycin in vitro. Proc. Natl. Acad. Sci. USA 58, 2385–2392 (1967 b)
Luzzatto, L., Apirion, D., Schlessinger, D.: Mechanism of action of streptomycin in E. coli: Interruption of the ribosome cycle at the initiation of protein synthesis. Proc. Natl. Acad. Sci. USA 60, 873–880 (1968)
Luzzatto, L., Apirion, D., Schlessinger, D.: Streptomycin action: Greater inhibition of Escherichia coli ribosome function with exogenous than with endogenous messenger ribonucleic acid. J. Bacteriol. 99, 206–209 (1969 a)
Luzzatto, L., Apiron, D., Schlessinger, D.: Polysome depletion and blockage of the ribosome cycle by streptomycin in Escherichia coli. J. Mol. Biol. 42, 315–335 (1969 b)
Mager, J., Benedict, M., Artman, M.: A common site of action for polyamines and streptomycin. Biochim. Biophys. Acta 62, 202–204 (1962)
Mahady, S.C., Armstrong, F.L., Beck, F., Horton, R., Lincoln, N.S.: A comparative study of streptomycin and dihydrostreptomycin in pulmonary tuberculosis. Am. Rev. Tuberc. 68, 238–248 (1953)
McGilveray, I.J., Rinehart, K.L., Jr.: Anomeric linkage of streptose in streptomycin and bluensomycin. J. Am. Chem. Soc. 87, 4003–4004 (1965)
Medeiros, A.A., O’Brien, T.F., Wacker, W.E.C., Yulug, N.F.: Effect of salt concentration on the apparent in vitro susceptibility of pseudomonads and other gram negative bacilli to gentamicin. J. Infect. Dis. 124, 59–64 (1971)
Miskin, R., Zamir, A.: Effect of streptomycin on ribosome interconversion, a possible basis for the action of the antibiotic. Nature (New Biol.) 238, 78–80 (1972)
Miyoshi, Y., Yamagata, H.: Sucrose-dependent spectinomycin resistant mutants of Escherichia coli. J. Bacteriol. 125, 142–148 (1975)
Mizuno, S., Nitta, K., Umezawa, H.: Mechanism of action of negamycin in E. coli K12. II. Miscoding activity in polypeptide synthesis directed by synthetic polynucleotide. J. Antibiot. 23, 589–594 (1970)
Mizuno, T., Yamada, H., Yamagata, H., Mizushima, S.: Coordinated alterations in ribosomes and cytoplasmic membrane in sucrose-dependent, spectinomycin-resistant mutants of Escherichia coli. J. Bacteriol. 125, 524–530 (1975)
Mizuno, T., Yamagata, H., Mizushima, S.: Interaction of cytoplasmic membrane and ribosomes in Escherichia coli: Spectinomycin-induced disappearance of membrane protein I-19. J. Bacteriol. 129, 326–332 (1977)
Modolell, J., Davis, B.D.: Rapid inhibition of polypeptide chain extension by streptomycin: Proc. Natl. Acad. Sci. USA 61, 1279–1286 (1968)
Modolell, J., Davis, B.D.: Mechanism of inhibition of ribosomes by streptomycin. Nature (London) 244, 345–348 (1969)
Modolell, J., Davis, B.D.: Breakdown by streptomycin of initiation complexes formed on ribosomes of Escherichia coli. Proc. Natl. Acad. Sci. USA 67, 1148–1155 (1970)
Morris, Y.J., Jennings, B.R.: The effect of neomycin and streptomycin on the electrical polarisability of aqueous suspensions of Escherichia coli. Biochim. Biophys. Acta 392, 328–334 (1975)
Neidle, S., Rogers, D., Hursthouse, M.B.: The crystal and molecular structure of streptomycin oxine selenate. Tetrahedron Lett. 1968, 4725–4728
Ninio, J.: A semi-quantitative treatment of missense and nonsense suppression in the strA and ram ribosomal mutants of Escherichia coli. Evaluation of some molecular parameters of translation in vivo. J. Mol. Biol. 84, 297–313 (1974)
Ninio, J.: Kinetic amplification of enzyme discrimination. Biochemie 57, 587–595 (1975)
Nomura, M., Engbaek, F.: Expression of ribosomal protein genes as analyzed by bacteriophage Mu-induced mutations. Proc. Natl. Acad. Sci. USA 69, 1526–1530 (1972)
Nomura, M., Sidikaro, J., Jakes, K., Zinder, N.: Effects of colicin E3 on bacterial ribosomes. In: Ribosomes. Nomura, M., Tissieres, A., Lengyel, P. (eds.), pp. 805–814. New York: Cold Spring Harbor 1974
Novak, E., Gray, J.E., Pfeifer, R.T.: Animal and human tolerance of high dose intramuscular therapy with spectinomycin. J. Infect. Dis. 130, 50–55 (1974)
Okamoto, S., Suzuki, Y.: Chloramphenicol-, dihydrostreptomycin- and kanamycin-inactivating enzymes from multiple drug-resistant Escherichia coli carrying episome ‘R’. Nature (London) 108, 1301–1303 (1965)
Okuyama, A., Watanabe, T., Tanaka, N.: Effects of aminoglycoside antibiotics on initiation of viral RNA-directed protein synthesis. J. Antibiot. 25, 212–218 (1972)
Ozaki, M., Mizushima, S., Nomura, M.: Identification and functional characterization of the protein controlled by the streptomycin-resistant locus in E. coli. Nature (London) 222, 333–339 (1969)
Ozanne, B., Benveniste, R., Davies, J.: Aminoglycoside antibiotics: Inactivation by phosphorylation in Escherichia coli carrying R factors. J. Bacteriol. 100, 1144–1146 (1969)
Pestka, S.: Inhibitors of protein synthesis. In: Molecular mechanisms of protein biosynthesis. Weissbach, H., Pestka, S. (eds.), pp. 467–553. New York, London: Academic Press 1977
Pestka, S., Marshall, R., Nirenberg, M.: RNA codewords and protein synthesis. V. Effects of streptomycin on the formation of ribosome-sRNA complexes. Proc. Natl. Acad. Sci. USA 53, 639–646 (1965)
Pinkett, M.O., Brownstein, B.L.: Streptomycin-induced synthesis of abnormal protein in an Escherichia coli mutant. J. Bacteriol. 119, 345–350 (1974)
Pittinger, C., Adamson, R.: Antibiotic blockade of neuromuscular function. Ann. Rev. Pharmacol. 12, 169–184 (1972)
Plötz, P.H., Davis, B.D.: Synergism between streptomycin and penicillin: A proposed mechanism. Science 135, 1067–1068 (1962)
Plötz, P.H., Dubin, D.T., Davis, B.D.: Influence of salts on the uptake of streptomycin by Escherichia coli. Nature (London) 191, 1324–1325 (1961)
Pölitz, S.M., Glitz, D.G.: Ribosome structure: localization of N6, N6-dimethyladenosine by electron microscopy of a ribosome-antibody complex. Proc. Natl. Acad. Sci. USA 74, 1468–1472 (1977)
Pongs, O., Erdmann, V.A.: Affinity labeling of E. coli ribosomes with a streptomycin-analogue. FEBS Lett. 37, 47–50 (1973)
Ramirez-Ronda, C.H., Holmes, R.K., Sanford, J.P.: Effect of divalent cations on binding of aminoglycoside antibiotics to human serum proteins and to bacteria. Antimicrob. Agents Chemother. 7, 238–245 (1975)
Rosenthal, S.L.: Aminoglycoside antibiotics. N.Y. State J. Med. 75, 535–547 (1975)
Rosset, R., Gorini, L.: A ribosomal ambiguity mutation. J. Mol. Biol. 39, 95–112 (1969)
Schatz, A., Bugie, E., Waksman, S.A.: Streptomycin, a substance exhibiting antibiotic activity against Gram-positive and Gram-negative bacteria. Proc. Soc. Exp. Biol. Med. 55, 66–69 (1944)
Schlessinger, D., Medoff, G.: Streptomycin, dihydrostreptomycin, and the gentamicins. In: Antibiotics. Corcoran, J.W., Hahn, F.E. (eds.), Vol. III, pp. 535–549. Berlin, Heidelberg, New York: Springer 1975
Schreiner, G., Nierhaus, K.H.: Protein involved in the binding of dihydrostreptomycin to ribosomes of Escherichia coli. J. Mol. Biol. 81, 71–82 (1973)
Schwartz, J.H.: An effect of streptomycin on the biosynthesis of coat protein of coliphage f2 by extracts of E. coli. Proc. Natl. Acad. Sci. USA 53, 1133–1140 (1965)
Sherman, M.I.: The role of ribosomal conformation in protein biosynthesis. Further studies with streptomycin. Eur. J. Biochem. 25, 291–300 (1972)
Sherman, M.I., Simpson, M.V.: The role of ribosomal conformation in protein biosynthesis: The streptomycin-ribosome interaction. Proc. Natl. Acad. Sci. USA 64, 1388–1395 (1969)
Shine, J., Dalgarno, L.: Determinant of cistron specificity in bacterial ribosomes. Nature (London) 254, 34–38 (1975)
Smith, D.H., Janjigian, J.A., Prescott, N., Anderson, P.W.: Resistance factor-mediated spectinomycin resistance. Infect. Immun. 1, 120–127 (1970)
Sparling, P.F., Davis, B.D.: Bactericidal action of streptomycin and comparison with spectinomycin in heterozygotes of Escherichia coli. Antimicrob. Agents. Chemother. 1, 252–258 (1972)
Sparling, P.F., Yobs, A.R., Billings, T.E., Hackney, J.F.: Spectinomycin sulphate and aqueous procaine penicillin G in treatment of female gonorrhea. Antimicrob. Agents Chemother. 689–692 (1965)
Sparling, P.F., Modolell, J., Takeda, Y., Davis, B.D.: Ribosomes from Escherichia coli merodiploids heterozygous for resistance to streptomycin and to spectinomycin. J. Mol. Biol. 37, 407–421 (1968)
Speyer, J.F., Langyel, P., Basilio, C.: Ribosomal localization of streptomycin sensitivity. Proc. Natl. Acad. Sci. USA 48, 684–686 (1962)
Spirin, A.S., Kostiashkina, O.E., Jonak, J.: Contribution of the elongation factors to resistance of ribosomes against inhibitors: comparison of the inhibitor effects on the factor-dependent and factor-free translation systems. J. Mol. Biol. 101, 553–562 (1976)
Spotts, C.R., Stanier, R.Y.: Mechanism of streptomycin action on bacteria: a unitary hypothesis. Nature (London) 192, 633–637 (1961)
Steitz, J.A., Jakes, K.: How ribosomes select initiator regions in mRNA: base pair formation between the 3′ terminus of 16 S RNA and the mRNA during initiation of protein synthesis in Escherichia coli. Proc. Natl. Acad. Sci. USA 72, 4734–4738 (1975)
Stern, J.L., Barner, H.D., Cohen, S.S.: The lethality of streptomycin and the stimulation of RNA synthesis in the absence of protein synthesis. J. Mol. Biol. 17, 188–217 (1966)
Stöffler, G., Wittmann, H.G.: Primary structure and three-dimensional arrangement of proteins within the Escherichia coli ribosomes. In: Molecular mechanisms of protein biosynthesis. Weissbach, H., Pestka, S. (eds.), p. 117–202. New York, London: Academic Press 1977
Stöffler, G., Deusser, E., Wittmann, H.G., Apirion, D.: Ribosomal proteins XIX. Altered S 5 ribosomal proteins in an Escherichia coli revertant from streptomycin dependence to independence. Mol. Gen. Genet. 111, 334–341 (1971)
Strigini, P., Gorini, L.: Ribosomal mutations affecting efficiency of amber suppression. J. Mol. Biol. 47, 517–530 (1970)
Tai, P.-C.: Impaired initiation complex formation on ribosomes treated with colicin E3. Biochem. Biophys. Res. Commun. 67, 1466–1472 (1975)
Tai, P.-C.: The interaction of streptomycin with ribosomes treated with colicin E3. Fed. Proc. 35, 1352 (1976)
Tai, P.-C., Davis, B.D.: Activity of colicin E3-treated ribosomes in initiation and in chain elongation. Proc. Natl. Acad. Sci. USA 71, 1021–1025 (1974)
Tai, P.-C., Wallace, B.J., Herzog, E.L., Davis, B.D.: Properties of initiation-free polysomes of Escherichia coli. Biochemistry 12, 609–615 (1973)
Tai, P.-C., Wallace, B.J., Davis, B.D.: Selective action of erythromycin on initiating ribosomes. Biochemistry 13, 4653–4659 (1974)
Tai, P.-C., Wallace, B.J., Davis, B.D.: Streptomycin causes misreading of natural messenger by interacting with ribosomes after initiation. Proc. Natl. Acad. Sci. USA 75, 275–279 (1978)
Takasawa, S., Utahara, R., Okanishi, M., Maeda, K., Umezawa, H.: Studies on adenylyl streptomycin, a product of streptomycin inactivated by E. coli carrying the R factor. J. Antibiot. 21, 477–484 (1968)
Thompson, R.C., Stone, P.J.: Proofreading of the codon-antibodon interaction on ribosomes. Proc. Natl. Acad. Sci. USA 74, 198–202 (1977)
Traub, P., Nomura, M.: Structure and function of E. coli ribosomes, V. Reconstitution of functionally active 30 S ribosomal particles from RNA and proteins. Proc. Natl. Acad. Sci. USA 59, 777–784 (1968)
Traut, R.R., Heimark, R.L., Sun, T.-T., Hershey, J.W.B., Bollen, A.: Protein topography of ribosomal subunits from Escherichia coli. In: Ribosomes. Nomura, M., Tissieres, A., Lengyel, P. (eds.), pp. 271–308. New York: Cold Spring Harbor 1974
Tseng, J.T., Bryan, L.E., Van den Elzen, H.M.: Mechanisms and spectrum of streptomycin resistance in a natural population of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 2, 136–141 (1972)
Turnock, G.: The action of streptomycin in a mutant of Escherichia coli with increased sensitivity to the antibiotic. Biochem. J. 118, 659–666 (1970)
Turnock, G., Erickson, S.K., Ackrell, B.A.C., Birch, B.: A mutant of Escherichia coli with a defect in energy metabolism. J. Gen. Microbiol. 70, 507–515 (1972)
Umezawa, H., Takasawa, S., Okanishi, M., Utahara, R.: Adenylstreptomycin, a product of streptomycin inactivated by E. coli carrying R factor. J. Antibiot. 21, 81–82 (1968)
Umezawa, S.: The chemistry and conformation of aminoglycoside antibiotics. In: Drug action and drug resistance in bacteria. Aminoglycoside antibiotics. Mitsuhashi, S. (ed.), Vol. 2. Univ. of Tokyo Press 1975
Umezawa, S., Takahashi, Y., Usui, T., Tsuchiya, T.: Total synthesis of streptomycin. J. Antibiot. 27, 997 (1974 a)
Umezawa, S., Tsuchiya, T., Yamasaki, T., Sano, H., Takahashi, Y.: Total synthesis of dihydrostreptomycin. J. Am. Chem. Soc. 96, 920–921 (1974 b)
van Duin, J., Kurland, C.G., Dondon, J., Grunberg-Manago, M.: Near neighbors of IF 3 bound to 30 S ribosomal subunits. FEBS Lett. 59, 287 (1975)
van Knippenberg, P.H., van Ravenswaay, J.C., Claasen, Grijm-Vos, M., Veldstra, H., Bosch, L.: Stimulation and inhibition of polypeptide synthesis by streptomycin in ribosomal systems of Escherichia coli, programmed with various messengers. Biochim. Biophys. Acta 95, 461–473 (1965)
Verly, W.G., Barbason, H., Dusart, J., Pepitpas-Dewandre, A.: A comparative study of the action of ethyl methanesulphonate and HNO2 on the mutation to streptomycin resistance of Escherichia coli K12. Biochim. Biophys. Acta 145, 752–762 (1967)
Vogel, Z., Vogel, T., Zamir, A., Elson, D.: Ribosome activation and the binding of dihydrostreptomycin: effect of polynucleotides and temperature on activation. J. Mol. Biol. 54, 379–386 (1970)
Walker, J.B.: Biosynthesis of the mono guanidinated inositol moiety of bluensomycin, a possible evolutionary precursor of streptomycin. J. Biol. Chem. 249, 2397–2404 (1974)
Wallace, B.J., Davis, B.D.: Cyclic blockade of initiation sites by streptomycin-damaged ribosomes in Escherichia coli: An explanation for dominance of sensitivity. J. Mol. Biol. 75, 377–390 (1973)
Wallace, B.J., Tai, P.-C., Davis, B.D.: Effect of streptomycin on the response of Escherichia coli ribosomes to the dissociation factor. J. Mol. Biol. 75, 391–400 (1973 a)
Wallace, B.J., Tai, P.-C., Herzog, E.L., Davis, B.D.: Partial inhibition of polysomal ribosomes of Escherichia coli by streptomycin. Proc. Natl. Acad. Sci. USA 70, 1234–1237 (1973 b)
Wallace, B.J., Tai, P.-C., Davis, B.D.: Selective inhibition of initiating ribosomes by spectinomycin. Proc. Natl. Acad. Sci. USA 71, 1634–1638 (1974)
Watanakunakorn, C., Bakie, C.: Synergism of vancomycin-gentamicin and vandomycin-streptomycin against enterococci. Antimicrob. Agents. Chemother. 4, 120–124 (1973)
Weinstein, L.: Streptomycin, gentamicin and other aminoglycosides. In: The pharmacological basis of therapeutics, Chap. 58. Goodman, L.S., Gilman, A. (ed.). London: Macmillan Co. 1975
White, J.R., White, H.L.: Streptomyeinoid antibiotics: synergism by puromycin. Science 146, 772–774 (1964)
Wilhelm, J.M., Corcoran, J.W.: Antibiotic glycosides. VI. Definition of the 50S ribosomal subunit of Bacillus subtilis 168 as a major determinant of sensitivity to erythromycin A. Biochemistry 6, 2578–2585 (1967)
Wittmann, H.G., Apirion, D., Analysis of ribosomal proteins in streptomycin resistant and dependent mutants isolated from streptomycin independent Escherichia coli strains. Mol. Gen. Genet. 141, 331–341 (1975)
Wolfe, A.D., Hahn, F.E.: Stability of ribosomes from streptomycin-exposed Escherichia coli. Biochem. Biophys. Res. Commun. 31, 945–949 (1968)
Wyatt, P.J., Berkman, R.M., Phillips, D.T.: Osmotic sensitivity in Staphylococcus aureus induced by streptomycin. J. Bacteriol. 110 (2), 523–528 (1972)
Yaguchi, M., Wittmann, H.G.: Cooperative control of translational fidelity by ribosomal proteins in Escherichia coli II. Localization of amino acid replacements in proteins S 5 and S 12 altered in double mutants resistant to neamine. Mol. Gen. Genet. 142, 35–43 (1975)
Yamada, T., Tipper, D., Davies, J.: Enzymic inactivation of streptomycin by R-factor-resistant Escherichia coli. Nature (London) 219, 288–291 (1968)
Yates, J.L., Gette, W.R., Furth, M.E., Nomura, M.: Effects of ribosomal mutations on the read-through of a chain termination signal: studies on the synthesis of bacteriophage λ O gene protein in vitro. Proc. Natl. Acad. Sci. USA 74, 689–693 (1977)
Zamir, A., Miskin, R., Elson, D.: Inactivation and reactivation of ribosomal subunits: aminoacyl-transfer RNA binding activity of the 30S subunit of Escherichia coli. J. Mol. Biol. 60, 347–364 (1971)
Zengel, J.M., Young, R., Dennis, P.P., Nomura, M.: Role of ribosomal protein S12 in peptide chain elongation: Analysis of pleiotropic streptomycin-resistant mutants of Escherichia coli. J. Bacteriol. 129, 1320–1329 (1976)
Zimelis, V.M., Jackson, G.G.: Activity of aminoglycoside antibiotics against Pseudomonas aeruginosa: specificity and site of calcium and magnesium antagonism. J. Infect. Dis. 127, 663–669 (1973)
Zimmerman, R.A., Garvin, R.T., Gorini, L.: Alteration of a 30S ribosomal protein accompanying the ram mutation in Escherichia coli. Proc. Natl. Acad. Sci. USA 68, 2263–2267 (1971 a)
Zimmerman, R.A., Moellering, R.C., Jr., Weinberg, A.N.: Mechanism of resistance to antibiotic synergism in enterococci. J. Bacteriol. 105, 873–879 (1971 b)
Zimmerman, R.A., Rosset, R., Gorini, L.: Nature of phenotypic masking exhibited by drug-dependent streptomycin A mutants of Escherichia coli. J. Mol. Biol. 57, 403–422 (1971 c)
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1979 Springer-Verlag Berlin · Heidelberg
About this chapter
Cite this chapter
Wallace, B.J., Tai, PC., Davis, B.D. (1979). Streptomycin 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_16
Download citation
DOI: https://doi.org/10.1007/978-3-642-46403-4_16
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-46405-8
Online ISBN: 978-3-642-46403-4
eBook Packages: Springer Book Archive