Abstract
A previous summary of chloramphenicol and its mode of action appeared in Vol I of the Mode of Action of Antibiotics. This review will chiefly concern the mode of action of chloramphenicol as currently understood and will concentrate on the work published since the previous volume. The previous review by Hahn (1967) has provided a summary of the work on chloramphenicol to that date. Other reviews published since that time also may be consulted for additional information (Weisblum and Davies, 1968; Pestka, 1971).
Keywords
- Protein Synthesis
- Cold Spring Harbor
- Chloramphenicol Resistance
- Peptide Bond Formation
- Amino Acid Incorporation
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References
Allen, E. H., and R. S. Schweet: Synthesis of hemoglobin in a cell-free system, I. Properties of the complete system. J. Biol. Chem. 237, 760–767 (1962).
Ambrose, C. T., and A. H. Coons: Studies on antibody production. VIII. The inhibitory effect of chloramphenicol on the synthesis of antibody in tissue culture. J. Exptl. Med. 117, 1075–1088 (1963).
Apirion, D., and D. Schlessinger: Coresistance to neomycin and kanamycin by mutations in an Escherichia coli Locus that affects ribosomes. J. Bacteriol. 96, 768–776 (1968).
Armentrout, S. A., and A. S. Weisberger: Inhibition of directed protein synthesis by chloramphenicol: Effect of magnesium concentration. Biochem. Biophys. Res. Commun. 26, 712–716 (1967).
Armentrout, S. A., and A. S. Weisberger: Ribonucleoprotein interaction with mammalian monosomes. Biochim. Biophys. Acta 161, 180–187 (1968).
Aronson, A. I., and S. Spiegelman: Protein and ribonucleic acid synthesis in a cloramphenicolinhibited system. Biochim. Biophys. Acta 53, 70–84 (1961a).
Aronson, A. I., and S. Spiegelman: On the nature of the ribonucleic acid synthesized in the presence of chloramphenicol. Biochim. Biophys. Acta 53, 84–95 (1961b).
Ashwell, M. A., and T. S. Work: Contrasting effects of cycloheximide on mitochondrial protein synthesis in vivo and in vitro. Biochem. Biophys. Res. Commun. 32, 1006–1012 (1968).
Ball, A. J. S., and E. R. Tustanoff: Effect of d(−) and l(+)-threo-chloramphenicol on nucleotide and related respiratory activities in yeast undergoing metabolic repression and de-repression. Biochim. Biophys. Acta 199, 476–489 (1970).
Borsook, H., E. H. Fischer, and G. Keighley: Factors affecting protein synthesis in vitro in rabbit reticulocytes. J. Biol. Chem. 229, 1059–1070 (1957).
Brenner, S., A. O. W. Stretton, and S. Kaplan: Genetic code: The “nonsense” triplets for chain termination and their suppression. Nature 206, 994–998 (1965).
Brock, T. D.: Chloramphenicol. Bacteriol. Rev. 25, 32–48 (1961).
Brock, T. D.: Chloramphenicol. Experimental chemotheraphy, vol. III, p. 119–169. New York: Academic Press, 1964.
Cameron, H. J., and G. R. Julian: The effect of chloramphenicol on the polysome formation of starved stringent Escherichia coli. Biochim. Biophys. Acta 169, 373–380 (1968).
Cannon, M.: The puromycin reaction and its inhibition by chloramphenicol. Eur. J. Biochem. 7, 137–145 (1968).
Capecchi, M. R.: Polypeptide chain termination in vitro: Isolation of a release factor. Proc. Natl. Acad. Sci. U.S. 58, 1144–1151 (1967a).
Capecchi, M. R.: A rapid assay for polypeptide chain termination. Biochem. Biophys. Res. Commun. 28, 773–778 (1967 b).
Capecchi, M. R., and H. A. Klein: Characterization of three proteins involved in polypeptide chain termination. Cold Spring Harbor Symp. Quant Biol. 34, 469–477 (1969).
Cashel, M.: The control of ribonucleic acid synthesis in E. coli IV. Relevance of unusual phosphorylated compounds from amino acid-starved stringent strains. J. Biol. Chem. 244, 3133–3141 (1969).
Cashel, M., and J. Gallant: Two compounds implicated in the function of the RC gene of E. coli. Nature 221, 838–841 (1969).
Cashel, M., and B. Kalbacher: The control of ribonucleic acid synthesis in E. coli V. Characterization of a nucleotide associated with the stringent response. J. Biol. Chem. 245, 2309–2318 (1970).
Caskey, T., R. Tompkins, E. Scolnick, T. Caryk, and M. Nirenberg: Sequential translation of trinucleotide codons for the initiation and termination of protein synthesis. Science 162, 135–138 (1968).
Celma, M. L., R. E. Monro, and D. Vazquez: Substrate and antibiotic sites at the peptidyl transferase centre of E. coli ribosomes. FEBS Letters 6, 273–277 (1970).
Černá, J., and I. Rychlik: Cross resistance of Escherichia coli B ribosomes to inhibition of the puromycin reaction by erythromycin, spiramycin and chloramphenicol. Biochim. Biophys. Acta 157, 436–438 (1968).
Černá, J., I. Rychlík, and P. Pulkrábek: The effect of antibiotics on the coded binding of peptidyl-tRNA to the ribosome and on the transfer of the peptidyl residue to puromycin. Eur. J. Biochem. 9, 27–35 (1969).
Chang, F. N., C. Siddhikol, and B. Weisblum: Subunit localization studies of antibiotic inhibitors of protein synthesis. Biochim. Biophys. Acta 186, 396–398 (1969).
Clark-Walker, G. D., and A. W. Linnane: In vivo differentiation of yeast cytoplasmic and mitochondrial protein synthesis with antibiotics. Biochem. Biophys. Res. Commun. 25, 8–13 (1966).
Clark-Walker, G. D., and A. W. Linnane: The biogenesis of mitochondria in Saccharomyces cerevisiae. A comparison between cytoplasmic respiratory-deficient mutant yeast and chloramphenicolinhibited wild type cells. J. Cell Biol. 34, 1–14 (1967).
Controulis, J., M. C. Rebstock, and H. M. Crooks: Chloramphenicol (Chloromycetin), V. Synthesis. J. Am. Chem. Soc. 71, 2463–2468 (1949).
Coutsogeorgopoulos, C.: On the mechanism of action of chloramphenicol in protein synthesis. Biochim. Biophys. Acta 129, 214–217 (1966).
Coutsogeorgopoulos, C.: Inhibitors of the reaction between puromycin and polylysyl-RNA in the presence of ribosomes. Biochem. Biophys. Res. Commun. 27, 46–52 (1967).
Coutsogeorgopoulos, C.: Amino acylaminonucleoside inhibitors of protein synthesis II. Effect on oligophenylalanine formation. Biochim. Biophys. Acta 240, 137–150; 247, 632 (1971).
Cross, D. F. W., G. W. Kenner, R. C. Sheppard, and C. E. Stehr: Peptides. Part XIV. Thiazole amino-acids degradation products of thiostrepton. J. Chem. Soc. 2143–2159 (1963).
Cruchaud, A., and A. H. Coons: Studies on antibody production. XIII. The effect of chloramphenicol on priming in mice. J. Exptl. Med. 120, 1061–1074 (1964).
Cundliffe, E., and K. McQuillen: Bacterial protein synthesis. The effects of antibiotics. J. Mol. Biol. 30, 137–146 (1967).
Das, H. K., A. Goldstein, and L. C. Kanner: Inhibition by chloramphenicol of the growth of nascent protein chains in Escherichia coli. Mol. Pharmacol. 2,. 158–170 (1966).
Davis, F. C., and B. H. Sells: Synthesis and assembly of ribosomal protein into 50S subunits during recovery from chloramphenicol treatment. J. Mol. Biol. 39, 503–521 (1969).
DeMoss, J. A., and G. D. Novelli: An amino acid dependent exchange between 32P labeled inorganic pyrophosphate and ATP in microbial extracts. Biochim. Biophys. Acta 22, 49–61 (1956).
Dixon, M.: The determination of enzyme inhibitor constants. Biochem. J. 55, 170–171 (1953).
Dresden, M. H., and M. B. Hoagland: Polyribosomes of Escherichia coli. Breakdown during glucose starvation. J. Biol. Chem. 242, 1065–1068 (1967).
Dresden, H. M., and M. B. Hoagland: Polyribosomes of Escherichia coli. Re-formation during recovery from glucose starvation. J. Biol. Chem. 242, 1069–1073 (1967).
Dunitz, J. D.: The crystal structure of chloramphenicol and bromamphenicol. J. Am. Chem. Soc. 74, 995–999 (1952).
Ehrenstein, G. von, and F. Lipmann: Experiments on hemoglobin biosynthesis. Proc. Natl. Acad. Sci. U.S. 47, 941–950 (1961).
Ellis, R. J., Chloroplast ribosomes; stereospecificity of inhibition by chloramphenicol. Science 163, 477–478 (1969).
Fernandez-Muñoz, R., R. E. Monro, R. Torres-Pinedo, and D. Vazquez: Substrate- and antibiotic-binding sites at the peptidyl-transferase centre of E. coli ribosomes. Studies on the chloramphenicol, lincomycin and erythromycin sites. Eur J. Biochem. 23, 185–193 (1971).
Fico, R., and C. Coutsogeorgopoulos: Peptidyl transferase. A new method for kinetic studies. Biochem. Biophys. Res. Commun. 47, 645–651 (1972).
Firkin, F. C., and A. W. Linnane: Differential effects of chloramphenicol on the growth and respiration of mammalian cells. Biochem. Biophys. Res. Commun. 32, 398–402 (1968).
Firkin, F. C., and A. W. Linnane: Biogenesis of mitochondria. VIII. The effect of chloramphenicol on regenerating rat liver. Exptl. Cell Res. 55, 68–76 (1969).
Flessel, C. P.: Chloramphenicol protects polyribosomes. Biochem. Biophys. Res. Commun. 32, 438–446 (1968).
Fraenkel, D. G., and F. C. Neidhardt: Use of chloramphenicol to study control of RNA synthesis in bacteria. Biochim. Biophys. Acta 53, 96–110 (1961).
Freeman, K. B.: Effects of chloramphenicol and its isomers and analogs on the mitochondrial respiratory chain. Can. J. Biochem. Physiol. 48, 469–478 (1970a).
Freeman, K. B.: Inhibition of mitochondrial and bacterial protein synthesis by chloramphenicol. Can J. Biochem. Physiol. 48, 479–485 (1970b).
Freeman, K. B., and D. Haldar: The inhibition of mammalian mitochondrial NADH oxidation by chloramphenicol and its isomers and analogs. Can. J. Biochem Physiol. 46, 1003–1008 (1968).
Frost, A. A., and R. G. Pearson: Kinetics and mechanisms, 233 pp. New York: Wiley & Sons 1953.
Gale, E. F.: Mechanisms of antibiotic action. Pharmacol. Rev. 15, 481–530 (1963).
Gale, E. F., and J. P. Folkes: The assimilation of amino-acids by bacteria. 15. Actions of antibiotics on nucleic acid and protein synthesis in Staphylococcus aureus. Biochem. J. 53, 493–498 (1953).
Galper, J. B., and J. E. Darnell: Mitochondrial protein synthesis in HeLa cells. J. Mol. Biol. 57, 363–367 (1971).
Gardner, R. S., A. J. Wahba, C. Basilio, R. S. Miller, P. Lengyel, and J. F. Speyer: Synthetic polynucleotides and the amino acid code. VII. Proc. Natl. Acad. Sci. U.S. 48, 2087–2094 (1962).
Godchaux, W., and E. Herbert: The effect of chloramphenicol in intact erythroid cells. J. Mol. Biol. 21, 537–553 (1966).
Goldberg, I. H.: Mode of action of antibiotics. II. Drugs affecting nucleic acid and protein synthesis. Am. J. Med. 39, 722–752 (1965).
Goldberg, I. H., and K. Mitsugi: Inhibition by sparsomycin and other antibiotics of the puromycin-induced release of polypeptide from ribosomes. Biochemistry 6, 383–391 (1967).
Gordon, P. A., M. J. Lowdon, and P. R. Stewart: Effects of chloramphenicol isomers and erythromycin on enzyme and lipid synthesis induced by oxygen in wild-type and petite yeast. J. Bacteriol. 110, 504–510 (1972).
Gottesman, M.: Reaction of ribosome-bound peptidyl transfer ribonucleic acid with aminoacyl transfer ribonucleic acid or puromycin. J. Biol. Chem. 242, 5564–5571 (1967).
Gros, F., J. Dubert, A. Tissieres, S. Bourgeois, M. Michelson, R. Soffer, and L. Legaalt: Regulation of metabolic breakdown and synthesis of messenger RNA in bacteria. Cold Spring Harbor Symp. Quant. Biol. 28, 299–313 (1964).
Gros, F., And F. Gros: Role Des Aminoacides Dans La Synthese Des Acides NucléIques Chez E. Coli. Biochim. Biophys. Acta 22, 200–201 (1956).
Gross, W., and K. Ring: Effect of chloramphenicol on active amino acid transport. FEBS Letters 4, 319–322 (1969).
Gurgo, C., D. Apirion, and D. Schlessinger: Effects of chloramphenicol and fusidic acid on polyribosome metabolism in Escherichia coli. FEBS Letters 3, 34–36 (1969a).
Gurgo, C., D. Apirion, and D. Schlessinger: Polyribosome metabolism in Escherichia coli treated with chloramphenicol, neomycin, spectinomycin or tetracycline. J. Mol. Biol. 45, 205–220 (1969 b).
Guthrie, G. D., and J. M. Buchanan: Control of phage-induced enzymes in bacteria. Federation Proc. 25, 864–873 (1966).
Hahn, F. E.: Chloramphenicol, antibiotics, vol. 1 (Gottlieb, D., Shaw, P.D., eds.) p. 308–330. Berlin-Heidelberg-New York: Springer 1967.
Hahn, F. E., J. E. Hayes, C. L. Wisseman, H. E. Hopps, and J. E. Smadel: Mode of action of chloramphenicol. VI. Relation between structure and activity in the chloramphenicol series. Antibiot. & Chemotherapy 6, 531–543 (1956).
Hahn, F. E., and C. L. Wisseman: Inhibition of adaptive enzyme formation by antimicrobial agents. Proc. Soc. Exptl. Biol. Med. 76, 533–535 (1951).
Haldar, D., and K. B. Freeman: The inhibition of protein synthesis and respiration in mouse ascites tumor cells by chloramphenicol and its isomers and analogs. Can. J. Biochem. Physiol. 46, 1009–1017 (1968).
Hamburger, R. N.: Chloramphenicol-specific antibody. Science 152, 203–204 (1966).
Hamburger, R. N., and J. H. Douglass: Chloramphenicol-specific antibody. II. Reactivity to analogues of chloramphenicol. Immunology 17, 587–591 (1969 a).
Hamburger, R. N., and J. H. Douglass: Chloramphenicol-specific antibody. IV. Neutralization of antibiotic effect on Escherichia coli. Immunology 17, 599–602 (1969 b).
Hishizawa, T., J. L. Lessard, and S. Pestka: Studies on the formation of transfer ribonucleic acid-ribosome complexes. XII. Phenylalanyl-oligonucleotide binding to E. coli ribosomes: Necessity for a free amino group. Proc. Natl. Acad. Sci. U.S. 66, 523–530 (1970).
Hishizawa, T., and S. Pestka: Studies on the formation of transfer ribonucleic acid-ribosome complexes. XVII. The effect of tRNA on aminoacyl-oligonucleotide binding to ribosomes. Arch. Biochem. Biophys. 147, 624–631 (1971).
Hori, M., and M. Rabinovitz: Polyribosomal changes during inhibition of rabbit hemoglobin synthesis by an isoleucine antagonist. Proc. Natl. Acad. Sci. U.S. 59, 1349–1355 (1968).
Hori, M., J. Suzuki, and H. Umezawa: Messenger RNA-associated 30S ribosomal subunit: Extraction from E. coli and the effect of chloramphenicol on the content. J. Biochem. (Tokyo) 64, 905–907 (1968).
Horowitz, J., and D. C. Hills: Evidence for the direct conversion of chloramphenicol particles into ribosomes in Escherichia coli. Biochim. Biophys. Acta 123, 416–419 (1966).
Hurwitz, C., and C. B. Braun: Measurement of binding of chloramphenicol by intact cells. J. Bacteriol. 93, 1671–1676 (1967).
Hurwitz, C., and C. B. Braun: Temperature-sensitivity of the weak bonds by which chloramphenicol is held in intact cells. Biochim. Biophys. Acta 157, 392–403 (1968).
Irvin, J. D., and G. R. Julian: The distribution of 14C-proline peptides synthesized in vitro directed by polycytidylic acid; the effect of chloramphenicol. FEBS Letters 8, 129–132 (1970).
Iyobe, S., H. Hashimoto, and S. Mitsuhashi: Integration of chloramphenicol-resistance gene of an R factor on Escherchia coli chromosome. Japan. J. Microbiol. 13, 225–232 (1969).
Iyobe, S., H. Hashimoto, and S. Mitsuhashi: Integration of chloramphenicol-resistance genes of an R factor into various sites of an Escherichia coli chromosome. Japan. J. Microbiol. 14, 463–471 (1970).
Jardetzky, O.: Studies on the mechanism of action of chloramphenicol, I. The conformation of chloramphenicol in solution. J. Biol. Chem. 238, 2498–2508 (1963).
Jardetzky, O., and G. Julian: Chloramphenicol inhibition of polyuridylic acid binding to E. coli ribosomes. Nature 201, 397–398 (1964).
Julian, G. R.: [14C]Lysine peptides synthesized in an in vitro Escherichia coli system in the presence of chloramphenicol. J. Mol. Biol. 12, 9–16 (1965).
Julian, G. R.: Effect of chloramphenicol on synthesis of C14-lysine peptides. Antimicrobial Agents Chemotherapy 1965, 992–1000 (1966).
Kaempfer, R.: Ribosomal subunit exchange during protein synthesis. Proc. Natl. Acad. Sci. U.S. 61, 106–113 (1968).
Kaempfer, R., and M. Meselson: Studies of ribosomal subunit exchange. Cold Spring Harbor Symp. Quant. Biol. 34, 209–220 (1969).
Kirschmann, C, and B. D. Davis: Phenotypic suppression in Escherichia coli by chloramphenicol and other reversible inhibitors of the ribosome. J. Bacteriol. 98, 152–159 (1969).
Kokolis, N., N. Mylonas, and I. Ziegler: Pteridine and riboflavin patterns during tail regeneration in Triturus species and the effects of chloramphenicol, isoxanthopterin and reserpine. Z. Naturforsch. 27b, 285–291 (1972 a).
Kokolis, N., N. Mylonas, and I. Ziegler: Pteridine and riboflavin in tumor tissue and the effect of chloramphenicol and isoxanthopterin. Z. Naturforsch. 27b, 292–295 (1972 b).
Kono, M., K. Ogawa, and S. Mitsuhashi: Drug resistance of staphylococci. VI. Genetic determinant for chloramphenicol resistance. J. Bacteriol. 95, 886–892 (1968).
Kono, M., K. O’Hara, M. Nagawa, and S. Mitsuhashi: Drug resistance of staphylococci: Ability of chloramphenicol related compounds to induce chloramphenicol resistance in Staphylococcus aureus. Japan. J. Microbiol. 15, 219–227 (1971).
Kroon, A. M.: Protein synthesis in heart mitochondria. I. Amino acid incorporation into the protein of isolated beef-heart mitochondria and fractions derived from them by sonic oscillation. Biochim. Biophys. Acta 72, 391–402 (1963).
Kucan, Z., and F. Lipmann: Differences in chloramphenicol sensitivity of cell-free amino acid polymerization systems. J. Biol. Chem. 239, 516–520 (1964).
Kurland, C. G.: The proteins of the bacterial ribosome. Protein synthesis: A series of advances, vol. 1 (McConkey, E., ed.), p. 179–228. New York: Marcel Dekker, 1971.
Kurland, C. G., and O. Maaloe: Regulation of ribosomal and transfer RNA synthesis. J. Mol. Biol. 4, 193–210 (1962).
Lacks, S., and F. Gros: A metabolic study of the RNA-amino acid complexes in Escherichia coli. J. Mol. Biol. 1, 301–320 (1959).
Lamborg, M. R., and P. C. Zamecnik: Amino acid incorporation into protein by extracts of E. coli. Biochim. Biophys. Acta 42, 206–211 (1960).
Lark, K. G.: Regulation of chromosome replication and segregation in bacteria. Bacteriol. Rev. 30, 3–32 (1966).
Lark, K. G. and C. Lark: Regulation of chromosome replication in E. coli: a comparison of the effects of phenethyl alcohol treatment with those of amino acid starvation. J. Mol. Biol. 20, 9–19 (1966).
Lazzarini, R. A., and R. M. Winslow: The regulation of RNA synthesis during growth rate transitions and amino acid deprivation in E. coli. Cold Spring Harbor Symp. Quant. Biol. 35, 383–390 (1970).
Lembach, K. J., and J. M. Buchanan: The relationship of protein synthesis to early transcriptive events in bacteriophage T4 Infected Escherichia coli B. J. Biol. Chem. 245, 1575–1587 (1970).
Lessard, J. L., and S. Pestka: Studies on the formation of transfer ribonucleic acid-ribosome complexes. XXII. Binding of aminoacyl-oligonucleotides to ribosomes. J. Biol. Chem. 247, 6901–6908 (1972 a).
Lessard, J. L., and S. Pestka: Studies on the formation of transfer ribonucleic acid-ribosome complexes XXIII. Chloramphenicol, aminoacyl-oligonucleotides, and Escherichia coli ribosomes. J. Biol. Chem. 247, 6909–6912 (1972 b).
Levine, A. J., and R. L. Sinsheimer: The process of infection with bacteriophage øXl74. XIX. Isolation and characterization of a chloramphenicol-resistant protein from øX-infected cells. J. Mol. Biol. 32, 567–578 (1968).
Levine, A. J., and R. L. Sinsheimer: The process of infection with bacterial phage øX174. XXVII. Synthesis of a viral-specific chloramphenicol-resistant protein in øX174 infected cells. J. Mol. Biol. 39, 655–668 (1969).
Levinthal, C., D. P. Fan, A. Higa, and R. A. Zimmerman: The decay and protection of messenger RNA in bacteria. Cold Spring Harbor Symp. Quant. Biol. 28, 183–190 (1964).
Linnane, A. W., A. J. Lamb, C. Christodolou, and H. B. Lukins: The biogenesis of mitochondria. VI. Biochemical basis of the resistance of Saccharomyces cerevisiae toward antibiotics which specifically inhibit mitochondrial protein synthesis. Proc. Natl. Acad. Sci. U.S. 59, 1288–1293 (1968).
Maaloe, O., and N. O. Kjeldgaard: Control of macromolecular biosynthesis. New York: W. A. Benjamin, Inc. 1966.
Marmur, J., and A. K. Saz: The inhibition of adaptive enzyme formation in Escherichia coli by chloramphenicol. Antibiot. & Chemotherapy 3, 613–617 (1953).
Maxwell, R. E., and V. S. Nickel: The antibacterial activity of the isomers of chloramphenicol. Antibiot. & Chemotherapy 4, 289–295 (1954).
Midgley, J. E. M., and W. J. H. Gray: The control of ribonucleic acid synthesis in bacteria. The synthesis and stability of ribonucleic acid in chloramphenicol-inhibited cultures of Escherichia coli. Biochem. J. 122, 149–159 (1971).
Mitsuhashi, S., M. Kono, M. Sagawa, and H. Mori: Drug resistance of staphylococcus: X. Induction of chloramphenicol resistance by its derivatives. Japan. J. Microbiol. 13, 177–180 (1969).
Monro, R. E.: Catalysis of peptide bond formation by 50S ribosomal subunits from Escherichia coli. J. Mol. Biol. 26, 147–151 (1967).
Monro, R. E.: The peptidyl transferase activity of ribosomes. Cold Spring Harbor Symp. Quant. Biol. 34, 357–366 (1969).
Monro, R. E., and K. A. Marcker: Ribosome-catalysed reaction of puromycin with a formylmethionine-containing oligonucleotide. J. Mol. Biol. 25, 347–350 (1967).
Monro, R. E., and D. Vazquez. Ribosome-catalysed peptidyl transfer: Effects of some inhibitors of protein synthesis. J. Mol. Biol. 28, 161–165 (1967).
Naha, P. M.: A chloramphenicol resistant host protein involved in lysogenization. Biochem. Biophys. Res. Commun. 35, 920–925 (1969).
Nasjleti, C. E., and H. H. Spencer: The effects of chloramphenicol on mitosis of phytohemagglutinin stimulated human leukocytes. Exptl. Cell Res. 53, 11–17 (1968).
Nathans, D.: Puromycin inhibition of protein synthesis: Incorporation of puromycin into peptide chains. Proc. Natl. Acad. Sci. U.S. 51, 585–592 (1964).
Nathans, D., Ehrenstein, G. von, R. Monro, and F. Lipmann: Protein synthesis from aminoacyl-soluble ribonucleic acid. Federation Proc. 21, 127–135 (1962).
Nathans, D., and F. Lipmann: Amino acid transfer from aminoacyl-ribonucleic acids to protein on ribosomes of Escherichia coli. Proc. Natl. Acad. Sci. U.S. 47, 497–504 (1961).
Nathans, D., and A. Neidle: Structural requirements for puromycin inhibition of protein synthesis. Nature 197, 1076–1077 (1963).
Newton, B. A.: Mechanisms of antibiotic action. Ann. Rev. Microbiol. 19, 209–240 (1965).
Nirenberg, M. W., and J. H. Matthaei: The dependence of cell-free protein synthesis in E. coli upon naturally occurring or synthetic polyribonucleotides. Proc. Natl. Acad. Sci. U.S. 47, 1588– 1602 (1961).
Nomura, M., and K. Hosokawa: Biosynthesis of ribosomes: Fate of chloramphenicol particles and of pulse-labeled RNA in Escherichia coli. J. Mol. Biol. 12, 242–265 (1965).
Nomura, M., and J. D. Watson: Ribonucleoprotein particles within chloromycetin-inhibited Escherichia coli. J. Mol. Biol. 1, 204–217 (1959).
Oerter, D., and R. Bass: Effect of chloramphenicol infusion on the rate of synthesis of cytochrome oxidase in mammalian embryonic tissue. Arch. Exptl. Pathol. Pharmakol. 272, 239–242 (1972).
Okamoto, S., and D. Mizuno: Inhibition by chloramphenicol of protein synthesis in the cell-free system of a chloramphenicol-resistant strain of Escherichia coli. Nature 195, 1022–1023 (1962).
Okamoto, S., and D. Mizuno: Mechanism of chloramphenicol and tetracycline resistance in Escherichia coli. J. Gen. Microbiol. 35, 125–133 (1964).
Okamoto, S., and Y. Suzuki: Chloramphenicol-, dihydrostreptomycin-, and kanamycin-inactivating enzymes from multiple drug-resistant Escherichia coli carrying episome ‘R’. Nature 208, 1301–1303 (1965).
Orgel, H. A., and R. N. Hamburger: Chloramphenicol-specific antibody. IV. A method for the detection of anti-chloramphenicol antibody in human sera. Immunology 20, 233–239 (1971).
Pardee, A. B., K. Paigen, and L. S. Prestidge: A study of the ribonucleic acid of normal and chloromycetin-inhibited bacteria by zone electrophoresis. Biochim. Biophys. Acta 23, 162–173 (1957).
Pardee, A. B., and L. S. Prestidge: The dependence of nucleic acid synthesis on the presence of amino acids in E. coli. J. Bacteriol. 71, 677–683 (1956).
Pestka, S.: Studies on the formation of transfer ribonucleic acid-ribosome complexes. V. On the function of a soluble transfer factor in protein synthesis. Proc. Natl. Acad. Sci. U.S. 61, 726–733 (1968).
Pestka, S.: Studies on the formation of transfer ribonucleic acid-ribosome complexes. VI. Oligopeptide synthesis and translocation on ribosomes in the presence and absence of souble transfer factors. J. Biol. Chem. 244, 1533–1539 (1969a).
Pestka, S.: Translocation, aminoacyl-oligonucleotides, and antibiotic action. Cold Spring Harbor Symp. Quant. Biol. 34, 395–410 (1969b).
Pestka, S.: Studies on the formation of transfer ribonucleic acid-ribosome complexes. X. Phenyl-alanyl-oligonucleotide binding to ribosomes and the mechanism of chloramphenicol action. Biochem. Biophys. Res. Commun. 36, 589–595 (1969c).
Pestka, S.: Studies on the formation of transfer ribonucleic acid-ribosome complexes. XI. Antibiotic effects on phenylalanyl-oligonucleotide binding to ribosomes. Proc. Natl. Acad. Sci. U.S. 64, 709–714(1969 d).
Pestka, S.: Studies on the formation of transfer ribonucleic acid-ribosome complexes. VIII. Survey of the effect of antibiotics on n-acetyl-phenylalanyl-puromycin formation: Possible mechanism of chloramphenicol action. Arch. Biochem. Biophys. 136, 80–88 (1970 a).
Pestka, S.: Studies on the formation of transfer ribonucleic acid-ribosome complexes. IX. Effect of antibiotics on translocation and peptide bond formation. Arch. Biochem. Biophys. 136, 89–96 (1970 b).
Pestka, S.: Inhibitors of ribosome function. Ann. Rev. Microbiol. 25, 487–562 (1971).
Pestka, S.: Studies on transfer ribonucleic acid-ribosome complexes. XIX. Effect of antibiotics on peptidyl-puromycin synthesis on polyribosomes from Escherichia coli. J. Biol. Chem. 247, 4669–4678 (1972).
Pestka, S., B. H. Heck, and E.M. Scolnick: A convenient assay for mono-, di, and oligophenyl-alanines. Anal. Biochem. 28, 376–384 (1969).
Pestka, S., T. Hishizawa, and J. L. Lessard: Studies on the formation of transfer ribonucleic acid-ribosome complexes. XIII. Aminoacyl-oligonucleotide binding to ribosomes: Characteristics and requirements. J. Biol. Chem. 245, 6208–6219 (1970).
Peterson, R. F., P. S. Cohen and H. L. Ennis: Properties of T4 messenger RNA synthesized in the absence of protein synthesis. Virology 48, 201–206 (1972).
Piffaretti, J. C., B. Allet, and J. S. Pitton: Analogy between in vivo and in vitro biological effect of chloramphenicol and its acetylated derivatives. FEBS Letters 11, 26–28 (1970).
Primakoff, P., and P. Berg: Stringent control of transcription of phage ø80psu3. Cold Spring Harbor Symp. Quant. Biol. 35, 391–396 (1970).
Rebstock, M. C., H. M. Crooks, J. Controulis, and Q. R. Bartz: Chloramphenicol (Chloromycetin). IV. Chemical studies. J. Am. Chem. Soc. 71, 2458–2462 (1949).
Rendi, R.: The effect of chloramphenicol on the incorporation of labeled amino acids into proteins by isolated subcellular fractions from rat liver. Exptl. Cell Res. 18, 187–189 (1959).
Rendi, R., and S. Ochoa: Effect of chloramphenicol on protein synthesis in cell-free preparation of Escherichia coli. J. Biol. Chem. 237, 3711–3713 (1962).
Richert, N. J. and J. D. Hare: Distinctive effects of inhibitors of mitochondrial function on Rous sarcoma virus replication and malignant transformation. Biochem. Biophys. Res. Commun. 46, 5–10 (1972).
Ringrose, P. S., and R. W. Lambert: The action of novel chloramphenicol analogues on prokaryotic and eukaryotic systems. Biochim. Biophys. Acta, 299, 374–384 (1973).
Rychík, I.: Release of lysine peptides by puromycin from polylysyl-transfer ribonucleic acid in the presence of ribosomes. Biochim. Biophys. Acta 114, 425–427 (1966).
Rychík, I., J. Cerná, S. Chladek, J. Zemlicka, and Z. Haladova: Substrate specificity of ribosomal peptidyl transferase: 2’(3’)-O-aminoacyl nucleosides as acceptors of the peptide chain on the amino acid site. J. Mol. Biol. 43, 13–24 (1969).
Sabin, A. B.: Different effects of chloramphenicol, dactinomycin, and streptovitacin A on synthesis of tumor and virion antigens in SV40 virus-infected cells. Proc. Natl. Acad. Sci. U.S. 55, 1141–1148 (1966).
Salser, W., A. Bolle, and R. Epstein: Transcription during bacteriophage T4 development: A demonstration that distant sub-classes of the “early” RNA appear at different times and that some are “turned off” at late times. J. Mol. Biol. 49, 271–295 (1970).
Sambrook, J. F., D. P. Fan, and S. Brenner: A strong suppressor specific for UGA. Nature 214, 452–453 (1967).
Sarabhai, A. S., A. O. W. Stretton, S. Brenner, and A. Bolle: Co-linearity of the gene with the polypeptide chain. Nature 201, 13–17 (1964).
Scolnick, E., R. Tompkins, T. Caskey, and M. Nirenberg: Release factors differing in specificity for terminator codons. Proc. Natl. Acad. Sci. U.S. 61, 768–774 (1968).
Shaw, W. V., D. W. Bentley, and L. Sands: Mechanism of chloramphenicol resistance in Staphylococcus epidermidis. J. Bacteriol. 104, 1095–1105 (1970).
Shemyakin, M. N.: Khimia Antibiotikov 1, Moscow Acad. Sci. USSR (1961).
Sinsheimer, R. L., C. A. Hutchinson, and B. Lindqvist: Bacterial phage øX174: viral functions. Molecular biology of viruses, ed. J. P. Colter and W. Paranchych, p. 175–192. New York: Academic Press 1967.
Sinsheimer, R. L., B. Starman, C. Nagler and S. Guthrie: The process of infection with bacteriophage øX174. I. Evidence for a “replicative” form. J. Mol. Biol. 4, 142–160 (1962).
So, A. G., and E. W. Davie: The incorporation of amino acids into protein in a cell-free system from yeast. Biochemistry 2, 132–136 (1963).
Sorm, F., and D. Grunberger: Inhibitory effect of chloramphenicol on the formation of some enzyme systems of Escherichia coli. Collection Czech. Chem. Commun. 19, 167–173 (1954).
Speyer, J. F., P. Lengyel, C. Basilio, A. J. Wahba, R. S. Gardner, and S. Ochoa: Synthetic polynucleotides and the amino acid code. Cold Spring Harbor Symp. Quant. Biol. 28, 559–567 (1963).
Stent, G. S., and S. Brenner: A genetic locus for the regulation of ribonucleic acid synthesis. Proc. Natl. Acad. Sci. U.S. 47, 2005–2014 (1961).
Stow, M., B. J. Starkey, I. C. Hancock and J. Baddiley: Inhibition by chloramphenicol of glucose transfer in teichoic acid biosynthesis. Nature New Biol. 229, 56–57 (1971).
Svehag, S.: Antibody formation in vitro by separated spleen cells. Inhibition by actinomycin or chloramphenicol. Science 146, 659–661 (1964).
Symons, R. H., R. J. Harris, L. P. Clarke, J. F. Wheldrake, and W. H. Elliott. Structural requirements for inhibition of polyphenylalanine synthesis by aminoacyl and nucleotidyl analogues of puromycin. Biochim. Biophys. Acta 179, 248–250 (1969).
Talal, N., and E. D. Exum: Two classes of spleen ribosomes with different sensitivities to chloramphenicol. Proc. Natl. Acad. Sci. U.S. 55, 1288–1295 (1966).
Tanaka, K., H. Teraoka, T. Nagira, and M. Tamaki: [14C]Erythromycin-ribosome complex formation and non-enzymatic binding of aminoacyl-transfer RNA to ribosome-messenger RNA complex. Biochim. Biophys. Acta 123, 435–437 (1966).
Taubman, S. B., N. R. Jones, F. E. Young, and J. W. Corcoran: Sensitivity and resistance to erythromycin in Bacillus subtilis 168: The ribosomal binding of erythromycin and chloramphenicol. Biochim. Biophys. Acta 123, 438–440 (1966).
Teraoka, H.: Reversal of the inhibitory action of chloramphenicol on the ribosomal peptidyl-transfer reaction by erythromycin. Biochim. Biophys. Acta 213, 535–537 (1970).
Teraoka, H., K. Tanaka, and M. Tamaki: The comparative study on the effects of chloramphenicol, erythromycin and lincomycin on polylysine synthesis in an Escherichia coli cell-free system. Biochim. Biophys. Acta 174, 776–778 (1969).
Tessman, E. S.: Mutants of bacteriophage S13 blocked in infectious DNA synthesis. J. Mol. Biol. 17, 218–236 (1966).
Tissiéres, A., D. Schlessinger, and F. Gros: Amino acid incorporation into proteins by Escherichia coli ribosomes. Proc. Natl. Acad. Sci. U.S. 46, 1450–1463 (1960)
Traut, R. R., and R. E. Monro: The puromycin reaction and its relation to protein synthesis. J. Mol. Biol. 10, 63–72 (1964).
Vazquez, D.: Antibiotics which affect protein synthesis: The uptake of 14C-chloramphenicol by bacteria. Biochem. Biophys. Res. Commun. 12, 409–413 (1963).
Vazquez, D.: The binding of chloramphenicol by ribosomes from Bacillus megaterium. Biochem. Biophys. Res. Commun. 15, 464–468 (1964).
Vazquez, D.: Binding of chloramphenicol to ribosomes. The effect of a number of antibiotics. Biochim. Biophys. Acta 114, 277–288 (1966 a).
Vazquez, D.: 16th Symp. Soc. Gen. Microbiol., p. 169–191 (1966b).
Vazquez, D.: Antibiotics affecting chloramphenicol uptake by bacteria. Their effect on amino acid incorporation in a cell-free system. Biochim. Biophys. Acta 114, 289–295 (1966c).
Vazquez, D.: Inhibitors of protein synthesis at the ribosome level; studies on their site of action. Life Sci. 6, 381–386 (1967).
Vogel, Z., A. Zamir, and D. Elson: The possible involvement of peptidyl transferase in the termination step of protein biosynthesis. Biochemistry 8, 5161–5168 (1969).
Waller, J. P., T. Erdös, F. LeMoine, S. Guttman, and E. Sandrin: Inhibition of protein synthesis by aminoacyl 3’ (2’)-adenosine. Biochim. Biophys. Acta 119, 566–580 (1966).
Weber, M. J., and J. A. DeMoss: The inhibition by chloramphenicol of nascent protein formation in E. coli. Proc. Natl. Acad. Sci. U.S. 55, 1224–1230 (1966).
Weber,M. J., and J. A. DeMoss: Inhibition of the peptide bond synthesizing cycle by chloramphenicol. J. Bacteriol. 97, 1099–1105 (1969).
Weigert, M. G., and A. Garen: Base composition of nonsense codons in E. coli. Nature 206, 992–994 (1965).
Weisberger, A. S., S. Armentrout, and S. Wolfe.: Protein synthesis by reticulocyte ribosomes. I. Inhibition of polyuridylic acid-induced ribosomal protein synthesis by chloramphenicol. Proc. Natl. Acad. Sci. U.S. 50, 86–93 (1963).
Weisberger, A. S., T. M. Daniel, and A. Hoffman: Suppression of antibody synthesis and prolongation of homograft survival by chloramphenicol. J. Exptl. Med. 120, 183–196 (1964).
Weisberger, A. S., and S. Wolfe: Effect of chloramphenicol on protein synthesis. Federation Proc. 23, 976–983 (1964).
Weisblum, B.: Macrolide resistance in Staphylococcus aureus. In: Drug action and drug resistance in bacteria. I. Macrolide Antibiotics (ed. by S. Mitsuhashi), p. 217–238. Baltimore: Univ. Park Press 1971.
Weisblum, B., and J. Davies: Antibiotic inhibitors of the bacterial ribosome. Bacteriol. Rev. 32, 493–528 (1968).
Weissbach, H., B. Redfield, and N. Brot: Studies on the reaction of n-acetyl-phenylalanyl-tRNA with puromycin. Arch. Biochem. Biophys. 127, 705–710 (1968).
Wintersberger, E.: Proteinsynthese in isolierten Hefe-Mitochondrien. Biochem. Z. 341, 409–419 (1965).
Wisseman, C. L., J. E. Smadel, F. E. Hahn, and H. E. Hopps: Mode of action of chloramphenicol. I. Action of chloramphenicol on assimilation of ammonia and on synthesis of proteins and nucleic acids in Escherichia coli. J. Bacteriol. 67, 662–673 (1954).
Wolfe, A. D., and F. E. Hahn: Mode of action of chloramphenicol. IX. Effects of chloramphenicol upon a ribosomal amino acid polymerization system and its binding to bacterial ribosome. Biochim. Biophys. Acta 95, 146–155 (1965).
Young, R. M., and D. Nakada: Defective ribosomes in chloramphenicol-treated Escherichia coli. J. Mol. Biol. 57, 457–473 (1971).
Yukioka, M., and S. Morisawa: Reversibility of chloramphenicol inhibition of the poly U directed polyphenylalanine synthesis by G factor and GTP. Biochem. Biophys. Res. Commun. 40, 1331– 1339 (1970).
Yukioka, M., and S. Morisawa: Enhancement of the phenylalanyl-oligonucleotide binding to the peptidyl recognition center of ribosomal peptidyl transferase and inhibition of the chloramphenicol binding to ribosomes. Biochim. Biophys. Acta 254, 304–315 (1971).
Yunis, A. A. and G. R. Bloomberg: Chloramphenicol toxicity: Clinical features and pathogenesis. Prog. Hematol. 4, 138–159 (1964).
Zinder, N. D., D. L. Engelhardt, and R. E. Webster: Punctuation in the genetic code. Cold Spring Harbor Symp. Quant. Biol. 31, 251–256 (1966).
Zipser, D.: UGA: A third class of suppressible polar mutants. J. Mol. Biol. 29, 441–445 (1967).
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Pestka, S. (1975). Chloramphenicol. In: Corcoran, J.W., Hahn, F.E., Snell, J.F., Arora, K.L. (eds) Mechanism of Action of Antimicrobial and Antitumor Agents. Antibiotics, vol 3. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-46304-4_25
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