Chloramphenicol Acetyltransferase: Enzymology and Molecular Biology

References

• Ehrlich J., Bartz Q. R., Smith R. M., Joslyn D. A., Burkholder P. R. Chloromycetin, a new antibiotic from a soil actinomycet. Science 1947; 106: 417
   PubMed Web of Science ®Google Scholar
• Rebstock M. C., Crooks H. M., Controulis J., Bartz Q. R. Chloramphenicol (Chloromycetin). IV. Chemical studie. J. Am. Chem. Soc. 1949; 71: 2458
   Web of Science ®Google Scholar
• Rebstock M. C. Antibiotic. Medicinal Chemistry, A. Burger. Interscience, New York 1960; 877
   Google Scholar
• Jardetzky O. Studies on the mechanism of action of chloramphenicol. I. The conformation of chloramphenicol in solutio. J. Biol. Chem. 1963; 238: 2498
   PubMed Web of Science ®Google Scholar
• Bustard T. M., Egan R. S., Perun J. J. Conformational studies on chloramphenicol and related molecule. Tetrahedron 1973; 29: 1961
   Web of Science ®Google Scholar
• Pongs O. Chloramphenico. Mechanism of Action of Antibacterial Drugs, F. E. Hahn. Springer Verlag, Berlin 1979; 26
   Google Scholar
• Tritton T. R. Ribosome-chloramphenicol interactions: a nuclear magnetic resonance stud. Arch. Biochem. Biophys. 1979; 197: 10
   PubMed Web of Science ®Google Scholar
• Gale E. F., Cundliffe E., Reynolds P. E., Richmond M. H., Waring M. J. The Molecular Basis of Antibiotic Action, 2nd ed. John Wiley & Sons, London 1981; 402
   Google Scholar
• Yunis A. A. Chloramphenicol-induced bone marrow suppressio. Semin. Hematol. 1973; 10: 225
   PubMed Web of Science ®Google Scholar
• Burns L. E., Hodgman J. E., Cass A. B. Fatal circulatory collapse in premature infants receiving chloramphenico. New Engl. J. Med. 1959; 261: 1318
   PubMed Web of Science ®Google Scholar
• Lietman P. S. Chloramphenicol and the neonate-1979 vie. Clin. Pharmacol. Ther. 1979; 6: 151
   Google Scholar
• Dajani A. S., Kauffman R. E. The renaissance of chloramphenico. Pediatr. Clin. North Am. 1981; 28: 195
   PubMed Web of Science ®Google Scholar
• Lietman P. D., White T. J., Shaw W. V. Chloramphenicol: an enzymological microassa. Antimicrob. Agents Chemother. 1976; 10: 347
   PubMed Web of Science ®Google Scholar
• Weber A. F., Opheim K. E., Koup J. R., Smith A. L. Comparison of enzymatic and liquid chromatographic chloramphenicol assay. Antimicrob. Agents Chemother. 1981; 19: 323
   PubMed Web of Science ®Google Scholar
• Nakano H., Tomita F., Suzuki T. Biosynthesis of corynecins by Corynebacterium hydrocarboclastuson the origin of the n-acyl grou. Agric. Biol. Chem. 1976; 40: 331
   Web of Science ®Google Scholar
• Watanabe T. Infective heredity of multiple drug resistance in bacteri. Bacteriol. Rev. 1963; 27: 87
   PubMedGoogle Scholar
• Datta N. Infectious drug resistanc. Br. Med. Bull. 1965; 21: 254
   PubMedGoogle Scholar
• Novick R. P., Richmond M. H. Nature and interactions of the genetic elements governing penicillinase synthesis i. S. aureus, J. Bacteriol. 1965; 90: 467
   PubMed Web of Science ®Google Scholar
• Anderson E. S. The ecology of transferable drug resistance in the Enterobacteri. Ann. Rev. Microbiol. 1968; 22: 131
   PubMed Web of Science ®Google Scholar
• Meynell E., Meynell G. G., Datta N. Phylogenetic relationships of drug-resistance factors and other transmissible bacterial plasmid. Bacteriol. Rev. 1968; 32: 55
   PubMedGoogle Scholar
• Novick R. P. Extrachromosomal inheritance in bacteri. Bacteriol. Rev. 1969; 33: 210
   PubMedGoogle Scholar
• Wolstenholme G. E. W., O'Connor M. Bacterial Episomes and Plasmids. Churchill, London 1969
   Google Scholar
• Clowes R. C. Molecular structure of bacterial plasmid. Bacteriol. Rev. 1972; 36: 361
   PubMedGoogle Scholar
• Davies J. E., Rownd R. Transmissible multiple drug resistance in Enterobacteriacea. Science 1972; 176: 758
   PubMed Web of Science ®Google Scholar
• Helinski D. R. Plasmid-determined resistance to antibiotics: molecular properties of R factor. Ann. Rev. Microbiol. 1973; 27: 437
   PubMed Web of Science ®Google Scholar
• Falkow S. Infectious Multiple Drug Resistance. Pion, London 1975
   Google Scholar
• Cohen S. N. Transposable genetic elements and plasmid evolutio. Nature 1976; 263: 731
   PubMed Web of Science ®Google Scholar
• Williams P. A. The biology of plasmid. Companion to Microbiology, A. T. Bull, P. M. Meadow. Longman, London 1978; 77
   Google Scholar
• Broda P. Plasmid. Freeman, Bristol 1979
   Google Scholar
• Timmis K. M. Gene manipulation in vitro i. Genetics as a Tool in Microbiology, S. W. Glover, D. A. Hopwood. Cambridge University Press, Cambridge 1981; 50
   Google Scholar
• Bukhari A. I., Shapiro J. A., Adhya S. L. DNA Insertion Element. Plasmids, and Episomes. Cold Spring Harbor Laboratory, New York 1977
   Google Scholar
• Novick R. P., Edelman I., Schwesinger M., Gruss A., Swanson E., Pattee P. A. Genetic translocation in Staphylococcus aureu. Proc. Natl. Acad. Sci. U.S.A. 1979; 76: 400
   PubMed Web of Science ®Google Scholar
• Starlinger P. IS elements and transposon. Plasmid 1980; 3: 241
   PubMed Web of Science ®Google Scholar
• Cullum J., Saedler H. DNA rearrangements and evolutio. Molecular and Cellular Aspects of Evolution, M. J. Carlile, J. F. Collins, B. E. B. Moseley. Cambridge University Press, Cambridge 1981; 131
   Google Scholar
• Okamoto S., Mizuno D. Mechanism of chloramphenicol and tetracycline resistance i. Escherichia coli, J. Gen. Microbiol. 1964; 35: 125
   PubMed Web of Science ®Google Scholar
• Miyamura S. Inactivation of chloramphenicol by chloramphenicol-resistant bacteri. J. Pharm. Sci. 1964; 53: 604
   PubMed Web of Science ®Google Scholar
• Shaw W. V. The enzymatic acetylation of chloramphenicol by extracts of R factor-resistan. Escherichia coli, J. Biol. Chem. 1967; 242: 687
   PubMed Web of Science ®Google Scholar
• Suzuki Y., Okamoto S. The enzymatic acetylation of chloramphenicol by the multiple drug-resistant Escherichia colicarrying R facto. J. Biol. Chem. 1967; 242: 4722
   PubMed Web of Science ®Google Scholar
• Dunsmoor C. L., Pim K. L., Sherris J. C. Observations on the inactivation of chloramphenicol by chloramphenicol-resistant staphylococci, in Antimicrobial Agents and Chemotherapy —196. American Society of Microbiology, J. C. Sylvester. Ann Arbor, Mich. 1964; 500
   Google Scholar
• Collins A. M., Roy T. E. Transduction of chloramphenicol and novobiocin resistance in staphylococc. Can. J. Microbiol. 1963; 9: 541
   Web of Science ®Google Scholar
• Goto S., Niwa C., Kuwahara S. Transduction of drug resistances in StaphylococcusII. Transduction of chloramphenicol resistance in both Staphylococcus aureusand Staphylococcus epidermidisby typing phage 8. Jpn. J. Microbiol. 1965; 9: 15
   PubMedGoogle Scholar
• Mitsuhashi S., Morimura M., Kono K., Oshima M. Elimination of drug resistance of Staphylococcus aureusby treatment with acrifiavin. J. Bacteriol. 1963; 86: 162
   PubMed Web of Science ®Google Scholar
• Chabbert Y. A., Baudens J. G., Gerbaud G. R. Variations caused by acriflavin and transduction of resistance to kanamycin and to chloramphenicol in staphylococc. Ann. Inst. Pasteur Paris 1964; 107(Suppl)678
   PubMedGoogle Scholar
• Suzuki Y., Okamoto S., Kono M. Basis of chloramphenicol resistance in naturally isolated resistant staphylococc. J. Bacteriol. 1966; 92: 798
   PubMed Web of Science ®Google Scholar
• Foster T. J., Shaw W. V. Chloramphenicol acetyltransferase specified by fi−R factor. Antimicrob. Agents Chemother. 1973; 3: 99
   PubMed Web of Science ®Google Scholar
• Sands L. C., Shaw W. V. Mechanism of chloramphenicol resistance in staphylococci: characterization and hybridization of variants of chloramphenicol acetyltransferas. Antimicrob. Agents Chemother. 1973; 3: 299
   PubMed Web of Science ®Google Scholar
• Shaw W. V., Sands L. C., Datta N. Hybridization of variants of chloramphenicol acetyltransferases specified by fi+and fi−R factor. Proc. Natl. Acad. Sci. U.S.A. 1972; 69: 3049
   PubMed Web of Science ®Google Scholar
• Foster T. J., Howe T. G. B. Chloramphenicol acetyltransferase formed by wild-type and complementing R factors in Escherichia coliK1. J. Gen. Microbiol. 1972; 71: 575
   PubMedGoogle Scholar
• Reeve E. C. R. Characteristics of some single-step mutants to chloramphenicol resistance in Escherichia coliK12 and their interaction with R factor gene. Genet. Res. 1966; 7: 281
   PubMedGoogle Scholar
• Foster T. J. R factor tetracycline and chloramphenicol resistance in Escherichia coliK12 and cmlB mutant. J. Gen. Microbiol. 1975; 90: 303
   PubMedGoogle Scholar
• Sompolinsky D., Samra Z. Mechanism of high-level resistance to chloramphenicol in different Escherichia colivariant. J. Gen. Microbiol. 1968; 50: 55
   PubMedGoogle Scholar
• Sompolinsky D., Ziegler-Schlomowritz R., Herezog D. Inactivation of chloramphenicol by Gram-negative microorganism. Can. J. Microbiol. 1968; 14: 891
   PubMed Web of Science ®Google Scholar
• Riley R., Anilionis A. Evolution of the bacterial genom. Ann. Rev. Microbiol. 1978; 32: 519
   PubMed Web of Science ®Google Scholar
• Nyman K., Nakamura K., Ohtsubo H., Ohtsubo E. Distribution of the insertion sequence ISI in Gram-negative bacteri. Nature 1981; 289: 609
   PubMed Web of Science ®Google Scholar
• Kono M., O'Hara K. Mechanism of chloramphenicol resistance mediated by kR102 facto. Pseudomonas aeruginosa, J. Antibiot. 1976; 29: 176
   PubMed Web of Science ®Google Scholar
• Nagai Y., Mitsuhashi S. New type of R factors incapable of inactivating chloramphenico. J. Bacteriol. 1972; 109
   PubMed Web of Science ®Google Scholar
• Gaffney D. F., Foster T. J., Shaw W. V. Chloramphenicol acetyltransferases determined by R plasmids from Gram-negative bacteri. J. Gen. Microbiol. 1978; 109: 351
   Google Scholar
• Gaffney D. F., Cundliffe E., Foster T. J. Chloramphenicol resistance that does not involve chloramphenicol acetyltransferase encoded by plasmids from Gram-negative bacteri. J. Gen. Microbiol. 1981; 125: 113
   PubMedGoogle Scholar
• Alton N. K., Vapnek D. Nucleotide sequence analysis of the chloramphenicol resistance transposon Tn. Nature 1979; 282: 864
   PubMed Web of Science ®Google Scholar
• Shaw W. V., Packman L. C., Burleigh B. D., Dell A., Morris H. R., Hartley B. S. Primary structure of a chloramphenicol acetyltransferase specified by bacterial plasmid. Nature 1979; 282: 870
   PubMed Web of Science ®Google Scholar
• Gottesman M. M., Rosner J. L. Acquisition of a determinant for chloramphenicol resistance by coliphage lambd. Proc. Natl. Acad. Sci. U.S.A. 1975; 72: 5041
   PubMed Web of Science ®Google Scholar
• Kondo E., Mitsuhashi S. Active transducing bacteriophage PI Cm by the combination of R factors with bacteriophage P. J. Bacteriol. 1964; 88: 1266
   PubMed Web of Science ®Google Scholar
• Bolivar F. Construction and characterization of new cloning vehicles. III. Derivatives of plasmid pBR322 carrying unique EcoRI sites for selection of EcoRI generated recombinant molecule. Gene 1978; 4: 121
   PubMed Web of Science ®Google Scholar
• Prentki P., Karch F., Iida S., Meyer J. The plasmid cloning vector pBR325 contains a 482-base pair-long inverted duplicatio. Gene 1981; 14: 289
   PubMed Web of Science ®Google Scholar
• Chang A. C. Y., Cohen S. N. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmi. J. Bacteriol. 1978; 134: 1141
   PubMed Web of Science ®Google Scholar
• Cohen S. N., Miller C. A. Nonchromosomal antibiotic-resistance in bacteria. II. molecular nature of R-factors isolated from Proteus mirabilis. Escherichia coli, J. Mol. Biol. 1970; 50: 671
   PubMed Web of Science ®Google Scholar
• Novick R. P., Clowes R. C., Cohen S. C., Curtiss R., Datta N., Falkow S. Uniform nomenclature for bacterial plasmids: a proposa. Bacteriol Rev. 1976; 40: 168
   PubMedGoogle Scholar
• Shaw W. V. Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteri. Methods Enzymol. 1975; 43: 737
   PubMedGoogle Scholar
• Packman L. C., Shaw W. V. Identification of buried lysine residues in two variants of chloramphenicol acetyltransferase specified by R-factor. Biochem. J. 1981; 193: 525
   PubMed Web of Science ®Google Scholar
• Packman L. C., Shaw W. V. The use of naturally occurring hybrid variants of chloramphenicol acetyltransferase to investigate subunit contact. Biochem. J. 1981; 193: 541
   PubMed Web of Science ®Google Scholar
• Liddell J. M., Shaw W. V., Swan J. D. A. Preliminary crystallographic data for a chloramphenicol acetyltransferase fro. Escherichia coli, J. Mol. Biol. 1978; 124: 285
   Web of Science ®Google Scholar
• Fitton J. E., Shaw W. V. Comparison of chloramphenicol acetyltransferase variants in staphylococc. Biochem. J. 1979; 177: 575
   PubMed Web of Science ®Google Scholar
• Guitard M., Daigneault R. Purification of Escherichia colichloramphenicol acetyltransferase by affinity chromatograph. Can. J. Biochem. 1974; 52: 1087
   PubMedGoogle Scholar
• Zaidenzaig Y., Shaw W. V. Affinity and hydrophobic chromatography of three variants of chloramphenicol acetyltransferase specified by R factors i. Escherichia coli, FEBS Lett. 1976; 62: 266
   PubMed Web of Science ®Google Scholar
• Horinouchi S., Weisblum B. Nucleotide sequence and functional map of pC194, a plasmid which specifies inducible chloramphenicol resistanc. J. Bacteriol. 1982; 150: 815
   PubMed Web of Science ®Google Scholar
• Shaw W. V. Enzymatic chloramphenicol acetylation and R factor induced antibiotic resistanc. Enterobacteriaceae in Antimicrobial Agents and Chemotherapy — 1966, G. L. Hobby. American Society of Microbiology, Ann Arbor, Mich. 1967; 221
   Google Scholar
• Shaw W. V., Brodsky R. F. Characterization of chloramphenicol acetyltransferase from chloramphenicol-resistan. Staphylococcus aureus, J. Bacteriol. 1968; 95: 28
   PubMed Web of Science ®Google Scholar
• Shaw W. V., Brodsky R. F. Chloramphenicol resistance by enzymatic acetylation: comparative aspect. Antimicrobial Agents and Chemotherapy — 1967, G. L. Hobby. American Society of Microbiology, Ann Arbor, Mich. 1968; 257
   Google Scholar
• Winshell E., Shaw W. V. Kinetics of induction and purification of chloramphenicol acetyltransferase from chloramphenicol-resistan. Staphylococcus aureus, J. Bacteriol. 1969; 98: 1248
   PubMed Web of Science ®Google Scholar
• Vazquez D. Mode of action of chloramphenicol and related antibiotic. Biochemical Studies of Antimicrobial Drugs, B. A. Newton, P. E. Reynolds. Cambridge University Press, Cambridge 1966; 169
   Google Scholar
• Freeman K. B. Inhibition of mitochondrial and bacterial protein synthesis by chloramphenico. Can. J. Biochem. 1970; 48: 479
   PubMedGoogle Scholar
• Kredich N. M., Becker M. A. Cysteine biosynthesis: serine transacetylase and O-acetyl serine sulfhydrylas. Salmonella typhimurium, Methods Enzymol. 1971; 17B: 459
   Google Scholar
• Hulanicka M. D., Kredich N. M. A mutation affecting expression of the gene coding for serine transacetylas. Salmonella typhimurium, Mol. Gen. Genet. 1976; 148: 143
   PubMed Web of Science ®Google Scholar
• Cook P. F., Wedding R. T. Cysteine synthetase from Salmonella typhimuriu. J. Biol. Chem. 1978; 253: 7874
   PubMed Web of Science ®Google Scholar
• Nagai S., Kerr D. Homoserine transacetylas. Methods Enzymol. 1971; 17B: 442
   Google Scholar
• Wyman A., Shelton E., Paulus H. Regulation of homoserine transacetylase in whole cells o. Bacillus polymyxa, J. Biol. Chem. 1975; 250: 3904
   PubMed Web of Science ®Google Scholar
• Zabin I., Fowler A. V. β-galactosidase, the lactose permease protein, and thiogalactoside transacetylas. The Operon., J. H. Miller, W. S. Reznikoff. Cold Spring Harbor, New York 1978; 89
   Google Scholar
• Kredich N. personal communication 1980
   Google Scholar
• Nagabhushan T. L., Kandasamy D., Tsai H., Turner W. N., Miller G. H. Novel class of chloramphenicol analogs with activity against chloramphenicol-resistant and chloramphenicol-susceptible organism. Current Chemotherapy and Infectious Diseases. American Society of Microbiology, Washington 1980; 442
   Google Scholar
• Syriopoulou V. P., Harding A. L., Goldman D. A., Smith A. L. In vitro antibacterial activity of fluorinated analogs of chloramphenicol and thiamphenico. Antimicrob. Agents Chemother. 1981; 19: 294
   PubMed Web of Science ®Google Scholar
• Harford S. personal communication 1980
   Google Scholar
• Shaw W. V., Bentley D. W., Sands L. Mechanism of chloramphenicol resistance in Staphylococcus epidermidi. J. Bacteriol. 1970; 104: 1095
   PubMed Web of Science ®Google Scholar
• Garber N., Zipser J. The inhibition of chloramphenicol-O-acetyl-transferase by adenine nucleotide. Biochim. Biophys. Acta 1970; 220: 341
   PubMedGoogle Scholar
• Nakagawa Y., Nitahara Y., Miyamura S. Kinetic studies on enzymatic acetylation of chloramphenicol in Streptococcus faecali. Antimicrob. Agents Chemother. 1979; 16: 719
   PubMed Web of Science ®Google Scholar
• Thibault G., Guitard M., Daigneault R. A study of the enzymatic inactivation of chloramphenicol by highly purified chloramphenicol acetyltransferas. Biochim. Biophys. Acta 1980; 614: 339
   PubMed Web of Science ®Google Scholar
• Nakagawa Y. Studies on enzymatic acetylation of chloramphenicol-resistant bacteria: GC-mass analysi. Jpn. J. Bacteriol. 1981; 36: 58
   Google Scholar
• Brent D. A., Chandrasurin P., Ragouzeos A., Hurlbert B. S., Burke J. T. Rearrangement of chloramphenicol-3-monosuccinat. J. Pharm. Sci. 1980; 69: 906
   PubMed Web of Science ®Google Scholar
• Kleanthous K., Shaw W. V. unpublished experiments 1981
   Google Scholar
• Shaw W. V., Unowsky J. Mechanism of R factor-mediated chloramphenicol resistanc. J. Bacteriol. 1968; 95: 1976
   PubMed Web of Science ®Google Scholar
• Piffaretti J.-C., Froment Y. Binding of chloramphenicol and its acetylated derivatives to Escherichia coliribosomal subunit. Chemotherapy 1978; 24: 24
   PubMed Web of Science ®Google Scholar
• Datta A., Rosner J. L. personal communication 1981
   Google Scholar
• Nordström K., Ingram L. C., Lundbäck A. Mutations in R factors of Escherichia coli, causing an increased number of R-factor copies per chromosom. J. Bacteriol. 1972; 110: 562
   PubMed Web of Science ®Google Scholar
• Shaw W. V. unpublished experiments 1987
   Google Scholar
• Jencks W. P., Cordes S., Carriuolo J. The free energy of thiol ester hydrolysi. J. Biol. Chem. 1960; 235: 3608
   PubMed Web of Science ®Google Scholar
• Bruice T. C., Benkovic S. Bio-organic Mechanisms. W. A. Benjamin, New York 1966; Vol. 1: 259
   Google Scholar
• Jencks W. P. Catalysis in Chemistry and Enzymology. McGraw-Hill, New York 1969; 517
   Google Scholar
• Jencks W. P. Handbook of Biochemistry and Molecular Biology, 3rd ed, G. D. Fasman. CRC Press, Cleveland, Ohio 1976; 296
   Google Scholar
• Tanaka H., Izaki K., Takahashi H. Some properties of chloramphenicol acetyltransferase, with particular reference to the mechanism of inhibition by basic triphenylmethane dye. J. Biochem. 1974; 76: 1009
   PubMed Web of Science ®Google Scholar
• Hersh L. B., Peet M. Re-evaluation of the kinetic mechanism of the choline acetyltransferase reactio. J. Biol. Chem. 1977; 252: 4796
   PubMed Web of Science ®Google Scholar
• Zaidenzaig Y., Shaw W. V. The reactivity of sulfhydryl groups at the active site of an R factor-specified variant of chloramphenicol acetyltransferas. Eur. J. Biochem. 1978; 83: 553
   PubMedGoogle Scholar
• Zaidenzaig Y., Fitton J. E., Packman L. C., Shaw W. V. Characterization and comparison of chloramphenicol acetyltransferase variant. Eur. J. Biochem. 1979; 100: 609
   PubMedGoogle Scholar
• Riddle B., Jencks W. P. Acetyl-coenzyme A: arylamine N-acetyltransferase. Role of the acetylenzyme intermediate and the effects of substituents on the rat. J. Biol. Chem. 1971; 246: 3250
   PubMed Web of Science ®Google Scholar
• Zaidenzaig Y., Shaw W. V. unpublished experiments 1976
   Google Scholar
• Corney A., Kleanthous K., Shaw W. V. Mechanism of chloramphenicol acetyltransferase: properties of a type III variant specified b. R plasmids in Gram-negative bacteria, in preparation.
   Google Scholar
• Albery W. J., Knowles J. R. Evolution of enzyme function and the development of catalytic efficienc. Biochemistry 1976; 15: 5631
   PubMed Web of Science ®Google Scholar
• Kucan Z., Lipmann F. Differences in chloramphenicol sensitivity of cell-free amino acid polymerization system. J. Biol. Chem. 1964; 239: 516
   PubMed Web of Science ®Google Scholar
• Marcoli R., Iida S., Bickle T. A. The DNA sequence of an IS-1-flanked transposon coding for resistance to chloramphenicol and fusidic aci. FEBS Lett. 1980; 110: 11
   PubMed Web of Science ®Google Scholar
• Nitzan (Zaidenzaig) Y., Gozhansky S. Chloramphenicol binding site of an fi−R-factor-specified variant of chloramphenicol acetyltransferas. Arch. Biochem. Biophys. 1980; 201: 115
   PubMed Web of Science ®Google Scholar
• Nakagawa Y., Bender M. L. Methylation of histidine-57 in α-chymotrypsin by methyl p nitrobenzene sulfonate. A new approach to enzyme modificatio. Biochemistry 1970; 9: 259
   PubMed Web of Science ®Google Scholar
• Melchior W. B., Fahrney D. Ethoxyformylation of proteins. Reaction of ethoxyformic anhydride with α-chymotrypsin, pepsin, and pancreatic ribonuclease at pH . Biochemistry 1970; 9: 251
   PubMed Web of Science ®Google Scholar
• Sonnenberg N., Wilchek M., Zamir A. Mapping of Escherichia coliribosomal components involved in peptidyltransferase activit. Proc. Natl. Acad. Sci. U.S.A. 1973; 70: 1423
   PubMedGoogle Scholar
• Pongs O., Bald R., Erdmann V. A. Identification of chloramphenicol binding protein in Escherichia coliribosomes by affinity labelin. Proc. Natl. Acad. Sci. U.S.A. 1973; 70: 2229
   PubMed Web of Science ®Google Scholar
• Pongs O., Messer W. The chloramphenicol receptor site in Escherichia coli.In vivo affinity labeling by monoiodoamphenico. J. Mol. Biol. 1976; 101: 171
   PubMed Web of Science ®Google Scholar
• Packman L. C. Studies on chloramphenicol acetyltransferases specified by R-factors. Ph.D. dissertation, University of Leicester. 1978
   Google Scholar
• Bennett P. M., Richmond M. H. Plasmids and their possible influence on evolutio. The Bacteria., J. R. Ornston Sokatch. Academic Press, New York 1978; Vol. VI: 1
   Google Scholar
• Cullum J., Saedler H. DNA rearrangements and evolutio. Molecular and Cellular Aspects of Microbial Evolution, M. J. Carlile, J. F. Collins, B. E. B. Moseley. Cambridge University Press, Cambridge 1981; 131
   Google Scholar
• Campbell A. Evolutionary significance of accessory DNA elements in bacteri. Annu. Rev. Microbiol. 1981; 35: 55
   PubMed Web of Science ®Google Scholar
• Jacobsen H. W., Shaw W. V. Chloramphenicol resistance in non-episoma. Proteus mirabilis, Bacteriol. Proc. 1970; 60, (Abstr.)
   Google Scholar
• Hall B. G., Zuzel T. Evolution of a new enzymatic function by recombination within a gen. Proc. Natl. Acad. Sci., U.S.A. 1980; 77: 3529
   PubMed Web of Science ®Google Scholar
• Clarke P. H. Experiments in microbial evolution: new enzymes, new metabolic activitie. Proc. R. Soc. London 1980; B 207: 385
   PubMed Web of Science ®Google Scholar
• Hall A., Knowles J. R. Directed selective pressure on a β-lactamase to analyze molecular changes involved in development of enzyme functio. Nature 1976; 264: 803
   PubMed Web of Science ®Google Scholar
• Hartley B. S. Evolution of enzyme structur. Proc. R. Soc. London Series B 1979; 205: 443
   PubMedGoogle Scholar
• Argoudelis A. D., Coats J. H. Microbial transformation of antibiotics. VI. Acylation of chloramphenicol by Streptomyces coelicolo. J. Antibiot. 1971; 24: 20
   Web of Science ®Google Scholar
• Shaw W. V., Hopwood D. A. Chloramphenicol acetylation in Streptomyce. J. Gen. Microbiol. 1976; 94: 159
   PubMedGoogle Scholar
• El-Kersh T. A., Plourde J. R. Biotransformation of Antibiotics. II. Investigation of the chloramphenicol acetyltransferase in Streptomyces griseu. J. Antibiot. 1976; 29: 1189
   PubMed Web of Science ®Google Scholar
• Harford S., Shaw W. V. Unpublished experiments 1977
   Google Scholar
• Wright H. M., Hopwood D. A. A chromosomal gene for chloramphenicol acetyltransferase in Streptomyces acrimycin. J. Gen. Microbiol. 1977; 102: 417
   PubMedGoogle Scholar
• Nakano H., Matsuhashi Y., Takeuchi T., Umezawa H. Distribution of chloramphenicol acetyltransferase and chloramphenicol-3-acetate esterase among Streptomycesand Corynebacteriu. J. Antibiot. 1977; 30: 76
   PubMed Web of Science ®Google Scholar
• Demain A. L. How do antibiotic-producing organisms avoid suicide?. Ann. N.Y. Acad. Sci. 1974; 235: 601
   PubMed Web of Science ®Google Scholar
• Lingens F., Oltmanns O. [Isolation and characterization of a chloramphenicol-destroying bacterium. Biochim. Biophys. Acta 1966; 130: 336
   PubMed Web of Science ®Google Scholar
• Haag R., Süssmuth R., Lingens F. The chloramphenicol resistance of a chloramphenicol degrading soil bacteriu. FEBS Lett. 1976; 63: 62
   PubMed Web of Science ®Google Scholar
• Süssmuth R., Haag R., Lingens F. Chloramphenicol resistance of three different Flavobacteri. J. Antibiot. 1979; 32: 1293
   PubMed Web of Science ®Google Scholar
• Beschle H. G., Süssmuth R., Lingens F. Conversion of chloramphenicol degradation products by tyrosine aminotransferase from Flavobacteri. Hoppe-Seyler's Z. Physiol. Chem. 1982; 363: 439
   PubMedGoogle Scholar
• Aber R. C., Wennersten C., Moellering R. C., Jr. Antimicrobial susceptibility of flavobacteri. Antimicrob. Agents Chemother. 1978; 14: 483
   PubMed Web of Science ®Google Scholar
• Currier T. C., Nester E. W. Evidence for diverse types of large plasmids in tumour inducing strains of Agrobacteriu. J. Bacteriol. 1976; 126: 157
   PubMed Web of Science ®Google Scholar
• Sciaky D., Montoya A. L., Chilton M.-D. Fingerprints of AgrobacteriumTi plasmid. Plasmid 1978; 1: 238
   PubMed Web of Science ®Google Scholar
• Burchard R. P., Parish J. H. Chloramphenicol resistance in Myxococcus xanthus, Antimicro. Agents Chemother. 1975; 7: 233
   PubMed Web of Science ®Google Scholar
• Brown N. L., Parish J. H. Extrachromosomal DNA in chloramphenicol resistant Myxococcus strain. J. Gen. Microbiol. 1976; 93: 63
   PubMedGoogle Scholar
• Eliopoulos E. personal communication 1981
   Google Scholar
• Cohen F. E., Richmond T. J., Richards F. M. Protein folding: evaluation of some simple rules for the assembly of helices into tertiary structures with myoglobin as an exampl. J. Mol. Biol. 1979; 132: 275
   PubMed Web of Science ®Google Scholar
• Cohen F. E., Sternberg M. J. E. On the use of chemically derived distance constraints in the prediction of protein structure with myoglobin as an exampl. J. Mol. Biol. 1980; 137: 9
   PubMed Web of Science ®Google Scholar
• Cohen F. E., Sternberg M. J. E., Taylor W. R. Analysis and prediction of protein β-sheet structures by a combinational approac. Nature 1980; 285: 378
   PubMed Web of Science ®Google Scholar
• Baumberg S. The evolution of metabolic regulatio. Molecular and Cellular Aspects of Microbial Evolution, M. J. Carlile, J. F. Collins, B. E. B. Moseley. Cambridge University Press, Cambridge 1981; 229
   Google Scholar
• Goldberg A. L., St. John A. C. Intracellular protein degradation in mammalian and bacterial cells: part . Ann. Rev. Biochem. 1976; 45: 747
   PubMed Web of Science ®Google Scholar
• Mosteller R. D., Goldstein R. V., Nishimoto K. R. Metabolism of individual proteins in exponentially growing Escherichia col. J. Biol. Chem. 1980; 255: 2534
   Web of Science ®Google Scholar
• Yen C., Green L., Miller C. G. Degradation of intracellular protein in Salmonella typhimuriumpeptidase mutant. J. Mol. Biol. 1980; 143: 21
   PubMed Web of Science ®Google Scholar
• Schneider W. P., Nichols B. P., Yanofsky C. Procedure for production of hybrid genes and proteins and its use in assessing significance of amino acid differences in homologous tryptophan synthetase α-polypeptide. Proc. Natl. Acad. Sci. U.S.A. 1981; 78: 2169
   PubMed Web of Science ®Google Scholar
• Iida S., Meyer J., Arber W. Genesis and natural history of ISI-mediated transposon. Cold Spring Harbor Symp. Quant. Biol. 1981; 45: 27
   PubMedGoogle Scholar
• Kondo E., Haapala D. K., Falkow S. The production of chloramphenicol acetyltransferase by bacteriophage PIC. Virology 1970; 40: 431
   PubMed Web of Science ®Google Scholar
• Rosner J. L., Guyer M. S. Transportation of ISI-λ B10-ISI from a bacteriophage λ derivative carrying the ISI-cat-ISI transposon (Tn9. Mol. Gen. Genet. 1980; 178: 111
   PubMedGoogle Scholar
• Chandler M., Boy de Ia Tour E., Willems D., Caro L. Some properties of the chloramphenicol resistance transposon Tn. Mol. Gen. Genet. 1979; 176: 221
   PubMedGoogle Scholar
• Iida S., Arber W. On the role of ISI in the formation of hybrids between the bacteriophage PI and the R plasmid NR. Mol. Gen. Genet. 1980; 177: 261
   PubMedGoogle Scholar
• Hashimoto H., Hirota Y. Gene recombination and segregation of resistance in Escherichia col. J. Bacteriol. 1966; 91: 51
   PubMed Web of Science ®Google Scholar
• Foster T. J., Howe T. G. B. Deletion map of the chloramphenicol resistance region of R1 and R10. J. Bacteriol. 1973; 116: 1062
   PubMed Web of Science ®Google Scholar
• Shaw W. V. Genetics and enzymology of chloramphenicol resistanc. Biochem. Soc. Trans. 1974; 2: 834
   Web of Science ®Google Scholar
• Harwood J., Smith D. H. Catabolite repression of chloramphenicol acetyltransferase synthesis in E. coliK1. Biochem. Biophys. Res. Commun. 1971; 42: 57
   PubMed Web of Science ®Google Scholar
• de Crombrugghe B., Pastan I., Shaw W. V., Rosner J. L. Stimulation by cyclic AMP and ppGpp of chloramphenicol acetyltransferase synthesi. Nature New Biol. 1973; 241: 237
   PubMedGoogle Scholar
• Dottin R. P., Shiner L. S., Hoar D. I. Adenosine 3′,5′-cyclic monophosphate regulation of chloramphenicol acetyltransferase synthesis in vitro from PICm DN. Virology 1973; 51: 509
   PubMed Web of Science ®Google Scholar
• Le Grice S. F. J., Matzura H. Localisation of the transcription initiation site of the chloramphenicol resistance gene on plasmid pAC18. FEBS Lett. 1980; 113: 42
   PubMed Web of Science ®Google Scholar
• Dempsey W. B., McIntire S. A. Lambda transducing phages derived from a Fin O−R100::λ cointegrate plasmid: proteins encoded by the R100 replication/incompatibility region and the antibiotic resistance determinan. Mol. Gen. Genet. 1979; 176: 319
   PubMedGoogle Scholar
• Iida S., Arber W. Plaque forming specialized transducing phage PI: Isolation of PICmSmSu, a precursor of PIC. Mol. Gen. Genet. 1977; 153: 259
   PubMedGoogle Scholar
• Meyer J., Iida S. Amplification of chloramphenicol resistance transposons carried by phage PICm in Escherichia col. Mol. Gen. Genet. 1979; 176: 209
   PubMedGoogle Scholar
• Iida S., Arber W. On the role of ISI in the formation of hybrids between the bacteriophage PI and the R plasmid NR. Mol. Gen. Genet. 1980; 177: 261
   PubMedGoogle Scholar
• Iida S. A cointegrate of the bacteriophage PI genome and the conjugative plasmid R10. Plasmid 1980; 3: 278
   PubMed Web of Science ®Google Scholar
• Iida S., Hänni C., Echarti C., Arber W. Is the ISI flanked r-determinant of the R plasmid NRI a transposon?. J. Gen. Microbiol. 1981; 126: 413
   PubMedGoogle Scholar
• Yanofsky C. Attenuation in the control of expression of bacterial operon. Nature 1981; 289: 751
   PubMed Web of Science ®Google Scholar
• Jaurin B., Grundström T., Edlund T., Normark S. The E. coliβ-lactamase attenuator mediates growth rate-dependent regulatio. Nature 1981; 290: 221
   PubMed Web of Science ®Google Scholar
• Davis R., Vapnek D. In vivo transcription of R-plasmid deoxyribonucleic acid in Escherichia colistrains with altered antibiotic resistance levels and/or conjugal proficienc. J. Bacteriol. 1976; 125: 1148
   PubMed Web of Science ®Google Scholar
• Alton N. K., Vapnek D. Transcription and translation of R-plasmid 538-I DNA: effects of mercury induction and analysis of polypeptides coded by the r-determinant regio. Plasmid 1979; 2: 366
   PubMed Web of Science ®Google Scholar
• Stüber D., Bujard H. Organization of transcriptional signals in plasmids pBR322 and pACYC18. Proc. Natl. Acad. Sci. U.S.A. 1981; 78: 167
   PubMed Web of Science ®Google Scholar
• Le Grice S. F. J., Matzura H. Binding of RNA polymerase and the catabolite gene activator protein within the catpromoter in Escherichia col. J. Mol. Biol. 1981; 150: 185
   PubMed Web of Science ®Google Scholar
• Le Grice S. F. J., Matzura H., Marcoli R., Iida S., Bickle T. A. The catabolite sensitive promoter for the chloramphenicol acetyltransferase gene is preceded by two binding sites for the catabolite gene activator protei. J. Mol. Biol. 1982; 150: 312
   Google Scholar
• de Crombrugghe B., Pastan I. Cyclic AMP, the cyclic AMP receptor protein, and the dual control of the galactose opero. The Operon, J. H. Miller, W. S. Reznikoff. Cold Spring Harbor Laboratory. 1978; 303
   Google Scholar
• McKay D. B., Steitz T. A. Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left handed B-DN. Nature 1981; 290: 744
   PubMed Web of Science ®Google Scholar
• O'Neill M. C., Amass K., de Crombrugghe B. Molecular model of the DNA interaction site for the cyclic AMP receptor protei. Proc. Natl Acad. Sci. U.S.A. 1981; 78: 2213
   PubMed Web of Science ®Google Scholar
• Enbright R. H., Wong J. R. Mechanism for transcriptional action of cyclic AMP in Escherichia colientry into DNA to disrupt DNA secondary structur. Proc. Natl. Acad. Sci. U.S.A. 1981; 78: 4011
   PubMed Web of Science ®Google Scholar
• Lee N. L., Gielow W. D., Wallace R. G. Mechanism of araC auto-regulation and the domains of two overlapping promoters, Pcand PBADin the L-arabinose regulatory pathway of Escherichia col. Proc. Natl. Acad. Sci. U.S.A. 1981; 78: 752
   PubMed Web of Science ®Google Scholar
• Völker T. A., Iida S., Bickle T. A. An single gene coding for resistance to both fusidic acid and chloramphenico. J. Mol. Biol. 1982; 154: 417
   PubMed Web of Science ®Google Scholar
• Martin J. F., Demain A. L. Control of antibiotic biosynthesi. Microbiol. Rev. 1980; 44: 230
   PubMedGoogle Scholar
• Datta N., Hedges R. W., Becker D., Davies J. Plasmid-determined fusidic acid resistance in the enterobacteriacea. J. Gen. Microbiol. 1974; 83: 191
   PubMedGoogle Scholar
• Dempsey W. B., Willetts N. S. Plasmid co-integrates of prophage lambda and R factor R10. J. Bacteriol. 1976; 126: 166
   PubMed Web of Science ®Google Scholar
• Lane D., Chandler M. Mapping of the drug resistance genes carried by the r-determinant of the R-100.1 plasmi. Mol. Gen. Genet. 1975; 157: 17
   Google Scholar
• Miki T., Easten A. M., Rownd R. H. Mapping of the resistance genes of NR. Mol. Gen. Genet. 1978; 158: 217
   PubMedGoogle Scholar
• Timmis K. N., Cabello F., Cohen S. N. Cloning and characterization of EcoRI and HindIII restriction endonuclease-generated fragments of antibiotic resistance plasmids R6–5 and R. Mol. Gen. Genet. 1978; 162: 121
   PubMedGoogle Scholar
• Bennett A. D., Shaw W. V. Resistance to fusidic acid in Escherichia colimediated by the type 1 variant of chloramphenicol acetyltransferas. submitted for publication.
   Google Scholar
• Proctor G. N., Rownd R. H. Rosanilins: indicator dyes for chloramphenicol resistant enterobacteria containing chloramphenicol acetyltransferas. J. Bacteriol., in press
   Google Scholar
• Coetzee J. N. Genetics of the Proteusgrou. Ann. Rev. Microbiol. 1972; 26: 23
   PubMedGoogle Scholar
• Cohen J. D., Eccleshall T. R., Needleman R. B., Federoff H., Buchferer B. A., Marmur J. Functional expression in yeast of the Escherichia coliplasmid gene coding for chloramphenicol acetyltransferas. Proc. Natl. Acad. Sci. U.S.A. 1980; 77: 1078
   PubMed Web of Science ®Google Scholar
• Goldfarb Doi D. S.R.H., Rodriguez R. L. The expression of Tn9-derived chloramphenicol resistanc. Bacillus subtilis, Nature 1981; 293: 309
   PubMed Web of Science ®Google Scholar
• Goldfarb D. S., Doi R. H., Close T. J., Rodriguez R. L. The development of an expression-vector in Bacillus subtilisusing a heterologous gen. Molecular Cloning and Gene Regulation in Bacilli, (Cetus-Stanford Conference). Academic Press. 1981
   Google Scholar
• de Crombrugghe B. personal communication 1981
   Google Scholar
• Gorman C. M., Moffat L. F., Howard B. H. Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cell. Mol. Cell Biol. 1981
   Web of Science ®Google Scholar
• Ehrlich S. D. Replication and expression of plasmids from Staphylococcus aureus. Bacillus subtilis, Proc. Natl. Acad. Sci. U.S.A. 1977; 74: 1680
   PubMed Web of Science ®Google Scholar
• Iordnescu S. Recombinant plasmid obtained from two different, compatible staphylococcal plasmid. J. Bacteriol. 1975; 124: 597
   PubMed Web of Science ®Google Scholar
• Iordnescu S., Surdeanu M., Della Latta P., Novick R. Incompatibility and molecular relationships between small staphylococcal plasmids carrying the same resistance marke. Plasmid 1978; 1: 468
   PubMed Web of Science ®Google Scholar
• Wilson C. R., Baldwin J. N. Characterization and construction of molecular cloning vehicles withi. Staphylococcus aureus, J. Bacteriol. 1978; 136: 402
   PubMed Web of Science ®Google Scholar
• Wilson C. R., Skinner S., Shaw W. V. Analysis of two chloramphenicol resistance plasmids from Staphylococcus aureusinsertional inactivation of Cm resistance, mapping of restriction sites, and construction of cloning vehicle. Plasmid 1981; 5: 245
   PubMed Web of Science ®Google Scholar
• Kono M., O'Hara K., Honda M., Mitsuhashi S. Drug resistance of staphylococci. XI. Induction of chloramphenicol resistance by its derivatives and analogue. J. Antibiot. 1969; 22: 603
   PubMed Web of Science ®Google Scholar
• Kono M., O'Hara K., Nagawa M., Mitsuhashi S. Drug resistance of staphylococci. Ability of chloramphenicol related compounds to induce chloramphenicol resistance in Staphylococcus aureus, Jp. J. Microbiol. 1971; 15: 219
   Web of Science ®Google Scholar
• Hawkins A., Fitton J. E., Skinner S. E., Shaw W. V. Chloramphenicol resistance in staphylococci: structure and expression of the gene for chloramphenicol acetyltransferase on plasmid pC22. in preparation.
   Google Scholar
• Gryczan T. J., Contente S., Dubnau D. Characterization of Staphylococcus aureusplasmids introduced by transformation int. Bacillus subtilis, J. Bacteriol. 1978; 134: 318
   PubMed Web of Science ®Google Scholar
• Löfdahl S., Sjostrom J.-E., Philipson L. Characterization of small plasmids fro. Staphylococcus aureus, Gene 1978; 3: 149
   Google Scholar
• Kono M., Sesatsu M., Hamashima H. Transformation of Bacillus subtiliswith plasmid DN. Microbios Lett. 1978; 5: 55
   Google Scholar
• Gryczan T. J., Dubnau D. Construction and properties of chimeric plasmid. Bacillus subtilis, Proc. Natl. Acad. Sci. U.S.A. 1978; 75: 1428
   PubMed Web of Science ®Google Scholar
• Goze A., Ehrlich S. D. Replication of plasmids from Staphylococcus aureu. Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 1980; 77: 7333
   PubMed Web of Science ®Google Scholar
• Pratt J. M., Boulnois G. J., Darby V., Orr E., Wahle E., Holland I. B. Identification of gene products programmed by restriction endonuclease DNA fragments using an E. coliin vitro syste. Nucl Acids Res. 1981; 9: 4459
   PubMed Web of Science ®Google Scholar
• Novick R. P., Brodsky R. F. Studies on plasmid replication. I. Plasmid incompatibility and establishmen. Staphylococcus aureus, J. Mol. Biol. 1972; 68: 285
   PubMed Web of Science ®Google Scholar
• Ishii K., Hashimoto-Gotoh T., Matsubara K. Slow segregation of mutants from multi-copy plasmid. Plasmid 1978; 1: 435
   PubMedGoogle Scholar
• Horinouchi S., Weisblum B. Nucleotide sequence and functional map of pE194, a plasmid which specifies inducible resistance to macrolide, lincosamide, and streptogramin type B antibiotic. J. Bacteriol. 1982; 150: 804
   PubMed Web of Science ®Google Scholar
• Miyamura S., Ochiai H., Nitahara Y., Nakagawa Y., Terao M. Resistance mechanism of chloramphenico. Streptococcus haemolyticus, Streptococcus pneumoniae, and Streptococcus faecalis, Microbiol. Immunol. 1977; 21: 69
   Web of Science ®Google Scholar
• Dang-Van A., Tiraby G., Acar J. F., Shaw W. V., Bouauchaud D. H. Chloramphenicol resistance in Streptococcus pneumoniaeenzymatic acetylation and possible plasmid linkag. Antimicrob. Agents Chemother. 1978; 13: 577
   PubMed Web of Science ®Google Scholar
• Robins-Brown R. M., Gaspar M. N., Ward J. I., Wachsmuth I. K., Koornhof H. J., Jacobs M. R., Thornsberry C. Resistance mechanisms of multiply resistant pneumococci: antibiotic degradation studie. Antimicrob. Agents Chemother. 1979; 15: 470
   PubMed Web of Science ®Google Scholar
• Shoemaker N. B., Smith M. D., Guild W. R. DNase-resistant transfer of chromosomal catand tetinsertions by filter matin. Pneumococcus, Plasmid 1980; 3: 80
   PubMed Web of Science ®Google Scholar
• Jacob A. E., Hobbs S. J. Conjugal transfer of plasmid-borne multiple antibiotic resistance in Streptococcus faecalisvar. zymogene. J. Bacteriol. 1974; 117: 360
   PubMed Web of Science ®Google Scholar
• van Embden J. D. A., Engel H. W. B., van Klingeren B. Drug resistance in Group D streptococci of clinical and non-clinical origin: prevalence, transferability, and plasmid propertie. Antimicrob. Agents Chemother. 1977; 11: 925
   PubMed Web of Science ®Google Scholar
• Courvalin P. M., Shaw W. V., Jacob A. E. Plasmid-mediated mechanisms of resistance to aminoglycoside-aminocyclitol antibiotics and to chloramphenicol in Group D streptococc. Antimicrob. Agents Chemother. 1978; 13: 716
   PubMed Web of Science ®Google Scholar
• Kono M., Hamashima H., Sasatsu M. Functional map of R plasmid (pTP51) resistant to multi-antibiotics isolated fro. Streptococcus faecalis, Microbios Lett. 1980; 14: 17–21
   Google Scholar
• Saunders C. W., Guild W. R. Pathway of plasmid transformation in Pneumococcusopen circular and linear molecules are activ. J. Bacteriol. 1981; 146: 517
   PubMed Web of Science ®Google Scholar
• Barany F., Tomasz A. Genetic transformation of Streptococcus pneumoniaeby heterologous plasmid deoxyribonucleic aci. J. Bacteriol. 1980; 144: 698
   PubMed Web of Science ®Google Scholar
• Weisblum B., Holder S. B., Halling S. M. Deoxyribonucleic acid sequence common to staphylococcal and streptococcal plasmids which specify erythromycin resistanc. J. Bacteriol. 1979; 138: 990
   PubMed Web of Science ®Google Scholar
• Lovett P. S. Personal communication 1981
   Google Scholar
• Keggins K. M., Lovett P. S., Duvall E. J. Molecular cloning of genetically active fragments of BacillusDNA in Bacillus subtilisand properties of the vector plasmid pUB11. Proc. Natl. Acad. Sci. U.S.A. 1978; 75: 1423
   PubMed Web of Science ®Google Scholar
• Dancer B. N. Transfer of plasmids among bacill. J. Gen. Microbiol. 1980; 121: 263
   PubMedGoogle Scholar
• Brown B. J., Carlton B. C. Plasmid-mediated transformation in Bacillus megateriu. J. Bacteriol. 1980; 142: 508
   PubMed Web of Science ®Google Scholar
• Martin P. A. W., Lohr J. R., Dean D. H. Transformation of Bacillus thuringiensisprotoplasts by plasmid deoxyribonucleic aci. J. Bacteriol. 1981; 145: 980
   PubMed Web of Science ®Google Scholar
• van Klingeren B. J., van Embden D. A., Dessens-Kroon M. Plasmid-mediated chloramphenicol resistanc. Haemophilus influenzae, Antimicrob. Agents Chemother. 1977; 11: 383
   PubMed Web of Science ®Google Scholar
• Shaw W. V., Bouanchaud D. H., Goldstein F. W. Mechanism of transferable resistance to chloramphenico. Haemophilus parainfluenzae, Antimicrob. Agents Chemother. 1978; 13: 326
   PubMed Web of Science ®Google Scholar
• Jahn G., Laufs R., Kaulfers P.-M., Kolenda H. Molecular nature of two Haemophilus influenzaeR factors containing resistances and the multiple integrations of drug resistance transposon. J. Bacteriol. 1979; 138: 584
   PubMedGoogle Scholar
• Roberts M. C., Smith A. L. Molecular characterization of “plasmid-free” antibiotic resistan. Haemophilus influenzae, J. Bacteriol. 1980; 144: 476
   PubMed Web of Science ®Google Scholar
• Koch A. L. Evolution of antibiotic resistance gene functio. Microbiol. Rev. 1981; 45: 355
   PubMedGoogle Scholar
• Thompson J., Cundliffe E. Purification and properties of an RNA methylase produced by Streptomyces agureusand involved in resistance to thiostrepto. J. Gen. Microbiol. 1981; 124: 291
   Google Scholar
• Pongs O. The receptor site for chloramphenicol in vitro and in viv. Drug Action at the Molecular Level, G. C. K. Roberts. Macmilian, London 1977; 190
   Google Scholar
• Sheehan J. C. Introductory remarks, in Penicillin Fifty Years After Flemin. Phil. Trans. R. Soc. Lond. 1980; B289: 165
   Google Scholar
• Chambliss G., Craven G. R., Davies J., Davis K., Kahan L., Nomura M. Ribosomes: Structure, Function, and Genetics. University Park Press, Baltimore 1980
   Google Scholar
• Auron P. E., Erdelsky K. J., Fahnestock S. R. Chemical modification studies of a protein at the peptidyltransferase site of the Bacillus stearothermophilusribosom. J. Biol. Chem. 1978; 253: 6893
   PubMed Web of Science ®Google Scholar
• Scolnick E., Milman G., Rosman M., Caskey T. Transesterification by peptidyl transferas. Nature 1970; 225: 152
   PubMedGoogle Scholar
• Fahnestock S., Neumann H., Shashoua V., Rich A. Ribosome-catalyzed ester formatio. Biochemistry 1970; 9: 2477
   PubMed Web of Science ®Google Scholar
• Harington C. Drug Resistance in Micro-organisms (Ciba Foundation Symposium), G. E. W. Wolstenholme, C. M. O'Connor. J. and A. Churchill, London 1957; 1
   Google Scholar
• Britz M. L., Wilkinson R. G. Chloramphenicol acetyltransferase of Bacteroides fragili. Antimicrob. Agents Chemother. 1978; 14: 105
   PubMed Web of Science ®Google Scholar
• Nagano K. Logical analysis of the mechanism of protein folding. I. Predictions of helices, loops, and β-structures from primary structur. J. Mol. Biol. 1973; 75: 401
   PubMed Web of Science ®Google Scholar
• Chou P. Y., Fasman G. D. Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from protein. Biochemistry 1974; 13: 211
   PubMed Web of Science ®Google Scholar
• Chou P. Y., Fasman G. D. Prediction of protein conformatio. Biochemistry 1974; 13: 222
   PubMed Web of Science ®Google Scholar
• Lim V. I. Structural principles of the globular organization of protein chains. A stereochemical theory of globular protein secondary structur. J. Mol. Biol. 1974; 88: 857
   PubMed Web of Science ®Google Scholar
• Lim V. I. Algorithms for prediction of α-helical and β-structural regions in globular protein. J. Mol. Biol. 1974; 88: 873
   PubMed Web of Science ®Google Scholar
• Burgess A. W., Ponnuswamy P. K., Scheraga H. A. Analysis of conformations of amino acid residues and prediction of backbone topography in protein. Isr. J. Chem. 1974; 12: 239
   Web of Science ®Google Scholar
• Chou P. Y., Fasman G. D. β-turns in protein. J. Mol. Biol. 1977; 115: 135
   PubMed Web of Science ®Google Scholar
• Duston M. J., Hider R. C. Snake toxin secondary structure prediction. J. Mol. Biol. 1977; 115: 177
   PubMed Web of Science ®Google Scholar
• Lenstra J. A., Hofsteenge J., Beintema J. J. Invariant features of the structure of pancreatic ribonucleas. J. Mol. Biol. 1979; 109: 185
   Google Scholar
• Garnier J., Osguthorpe D. J., Robson B. Analysis of the accuracy and implications of simple methods for predicting the secondary structures of globular protein. J. Mol. Biol. 1978; 120: 97
   PubMed Web of Science ®Google Scholar
• Guiney D. G., Davis C. E. Incompatibility and host range of p GD 10 fro. Capnocytophagia ochraceus, Plasmid, in press
   Google Scholar
• Nitzan Y., Rushansky N. Chloramphenicol acetyltransferase from Pseudomonas aeruginosa— a new variant of the enzym. Curr. Microbiol. 1981; 5: 259
   Web of Science ®Google Scholar
• Betz J. L., Sadler J. R. Variants of a cloned synthetic lactose operator. II. Chloramphenicol-resistant revertants retaining a lactose operator in the CAT gene of plasmid pBR32. Gene 1981; 15: 187
   PubMed Web of Science ®Google Scholar
• McLaughlin J. R., Murray C. L., Rabinowitz J. C. Unique features in the ribosome binding site sequence of the Cram-positive Staphylococcus aureusβ-lactamase gen. J. Biol. Chem. 1981; 256: 11283
   PubMed Web of Science ®Google Scholar
• McLaughlin J. R., Murray C. L., Rabinowitz J. C. Plasmid-directed expression of Staphylococcus aureusβ-lactamase by Bacillus subtilisin vitr. J. Biol. Chem. 1981; 256: 11273
   Web of Science ®Google Scholar
• Polak J., Novick R. P. Closely related plasmids from Staphylococcus aureusand soil bacteri. Plasmid 1982; 7: 152
   PubMed Web of Science ®Google Scholar
• Roberts M., Corney A., Shaw W. V. Molecular characterization of three chloramphenicol acetyltransferases isolated from Haemophilus influenza. J. Bacteriol. 1982; 151: 737
   PubMed Web of Science ®Google Scholar