Summary
Under conditions of derepression,Escherichia coli K12 strains diploid for thetrp operon specify more than twice as much enzyme as a haploid. The disproportionate increase probably occurs because episomally carriedtrp genes tend to specify more enzyme than do chromosomal genes.
Operons harboring the nonsense mutationtrpA2 or the missense mutationtrpBYS-101 specify less protein than do wild-type operons. This effect varies with operon location in the case oftrpBYS-101.
In a homozygoustrp merodiploid A46/F′ A46 reversion totrp + occurs three times as frequently in episomal DNA as in chromosomal DNA. Thus, if the chromosome: F′trp episome ratio inE. coli is one, as demonstrated by Helinski and co-workers, the rate of gene expression and the rate of mutation can vary and depends upon the location of the DNA within the cell.
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References
Adelberg, E. A., Myers, J. W.: Modification of the penicillin technique for the selection of auxotrophic bacteria. J. Bact.65, 348 (1958).
Cassio, D., Lawrence, F., Lawrence, D. A.: Level of methionyl-t-RNA synthetase in merodiploids ofEscherichia coli K12. Europ. J. Biochem.15, 331 (1970).
Crawford, I. P.: Identification of the triose phosphate formed in the tryptophan synthetase reaction. Biochim. biophys. Acta (Amst.)45, 405 (1960).
—, Sikes, S.: Mutants ofEscherichia coli defective in the B protein of tryptophan synthetase IV: Recombinational map. Genetics66, 607 (1970).
—— Belser, N. O., Martinez, L.: Mutants ofEscherichia coli defective in the B protein of tryptophan synthetase. III. Intragenic Clustering. Genetics65, 201 (1970).
— Yanofsky, C.: On the separation of the tryptophan synthetase ofEscherichia coli into two protein components. Proc. nat. Acad. Sci. (Wash.)44, 1161 (1958).
Creighton, R. E., Yanofsky, C.: Indole-3-glycerol phosphate synthetase ofEscherichia coli, an enzyme of the tryptophan operon. J. biol. Chem.241, 4616 (1966).
Fredericq, P.: The recombination of colicinogenic factors with other episomes and plasmids. In: Bacterial episomes and plasmids, ed. by G. E. W. Wolstenholme and M. O'Connor. Boston: Little, Brown and Co. 1969.
Garen, A., Garen, S.: Complementationin vivo between structural mutants of alkaline phosphatase fromE. coli. J. molec. Biol.7, 13 (1963).
Goldberg, M. E., Creighton, T. E., Baldwin, R. L., Yanofsky, C.: Subunit structure of the tryptophan synthetase ofEscherichia coli. J. molec. Biol.21, 71 (1966).
Held, W. A., Smith, O. H.: Mechanism of 3-methyl anthranilic acid derepression of the tryptophan operon inEscherichia coli. J. Bact.101, 209 (1970).
Henning, U., Helinski, D. R., Chao, F. C., Yanofsky, C.: The A protein of the tryptophan synthetase ofEscherichia coli. Purification, crystallization and composition studies. J. biol. Chem.237, 1523 (1962).
Hickson, R. F., Roth, T. F., Helinski, D. R.: Circular DNA forms of a bacterial sex factor. Proc. nat. Acad. Sci. (Wash.)58, 1731 (1967).
Ito, S., Crawford, I. P.: Regulation of the enzymes of the tryptophan pathway inEscherichia coli. Genetics52, 1303 (1965).
Jacob, F., Brenner, S., Cuzin, F.: On the regulation of DNA replication in bacteria. Cold Spr. Harb. Symp. quant. Biol.28, 329 (1963).
—, Monod, J.: On the regulation of gene activity. Cold Spr. Harb. Symp. quant. Biol.26, 193 (1961)
Lennox, E. S.: Transduction of linked genetic characters of the host by bacteriophage Pl. Virology1, 190 (1955).
Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, R. J.: Protein measurement with the folin phenol reagent. J. biol. Chem.193 265 (1951).
Matsushiro, A.: On the transcription of the tryptophan operon inEscherichia coli. I. The tryptophan operator. J. molec. Biol.11, 54 (1965).
Morse, D. E., Baker, R. F. Yanofsky, C.: Translation of the tryptophan messenger RNA ofEscherichia coli. Proc. nat. Acad. Sci. (Wash.)60, 1428 (1968).
— Yanofsky, C.: Amber mutants of the trp R regulatory gene. J. molec. Biol.44, 185 (1969).
Pittard, J., Ramakrishnan, T.: Gene transfer by F′ strains ofEscherichia coli. IV. Effect of a chromosomal deletion on chromosome transfer. J. Bact.88, 367 (1964).
Revel, H. R., Luria, S. E.: On the mechanism of unrepressed galactosidase synthesis controlled by a transducing phage. Cold Spr. Harb. Symp. quant. Biol.28, 403 (1963).
Rose, J. K., Mosteller, R. D., Yanofsky, C.: Tryptophan messenger ribonucleic acid elongation rates and steady-state levels of tryptophan operon enzymes under various growth conditions. J. molec. Biol.51, 541 (1970).
Somerville, R. L., Yanofsky, C.: Studies on the regulation of tryptophan biosynthesis inEscherichia coli. J. molec. Biol.11, 747 (1965).
Sparling, R. F., Modolell, J., Takeda, Y., Davis, B. D.: Ribosomes fromEscherichia coli merodiploids heterozygous for resistance to streptomycin and to spectinomycin. J. molec. Biol.37, 407 (1968).
Vogel, H. J., Bonner, D. M.: Acetylornithinase ofEscherichia coli: Partial purification and some properties. J. biol. Chem.218, 97, (1956).
Whitfield, H. J., Jr., Martin, R. G., Ames, B. N.: Classification of aminotransferase (C Gene) mutants in the histidine operon. J. molec. Biol.21, 335 (1966).
Yanofsky, C.: Enzymatic studies with a series of tryptophan auxotrophs ofEscherichia coli. J. biol. Chem.244, 783 (1957).
—: Amino acid replacements associated with mutation and recombination in the A gene and their relationship toin vitro coding data. Cold Spr. Harb. Symp. quant. Biol.28, 581 (1963).
— Ito, J.: Nonsense codons and polarity in the tryptophan operon. J. molec. Biol.21, 313 (1966).
——: Orientation of antipolarity in the tryptophan operon ofEscherichia coli. J. molec. Biol.24, 143 (1967).
Yura, T., Imai, M., Okamoto, T., Hiraga, S.: Transcription of the tryptophan operon ofEscherichia coli in vitro. I. Detection and quantitative determination of specific RNA. Biochim. biophys. Acta (Amst.)169, 494 (1968).
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Communicated by W. Maas
Supported by Grant AM-12150 from the National Institutes of Health. Journal Paper No. 3973 of Purdue Agricultural Experiment Station.
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Stetson, H., Somerville, R.L. Expression of the tryptophan operon in merodiploids ofEscherichia coli . Molec. Gen. Genet. 111, 342–351 (1971). https://doi.org/10.1007/BF00569786
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DOI: https://doi.org/10.1007/BF00569786