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A partial deletion map of the galactose operon in E. coli K12

Published online by Cambridge University Press:  14 April 2009

John Davison
Affiliation:
Institute of Animal Genetics, King's Buildings, West Mains Road, Edinburgh
Robin Frame
Affiliation:
Institute of Animal Genetics, King's Buildings, West Mains Road, Edinburgh
John Bishop
Affiliation:
Institute of Animal Genetics, King's Buildings, West Mains Road, Edinburgh
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We have isolated a number of λ dg HFT lysates which carry proximal fragments of the galactose operon. Most of these have been shown to be different, and each terminates in either the kinase or transferase cistron. They divide the kinase cistron genetically into seven blocks of mutants, and the transferase into eight.

When a λ dg is used to transduce a bacterium which carries a mutation in a cistron which is intact in the λ dg the transduction frequency is high in the presence of λ-helper. This is attributed to integration of the transducing fragment at the λ-attachment site and complementation between the two operons in the heterogenote. When the same λ dg transduces a mutation lying in the cistron in which the λ dg terminates, so that recombination within the galactose operon is obligatory, the transduction frequency is 10 to 1000 times less.

In such cases there is a general increase in transduction frequency between distal mutations (i.e. those lying near the termination of the deletion) and proximal mutations, but the relationship does not hold for many individual pairs of mutants, probably due to physiological differences between the bacterial strains.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1967

References

REFERENCES

Adler, J. & Kaiser, A. D. (1963). Mapping of the galactose genes of Escherichia coli by transduction with phage P1. Virology, 19, 117126.CrossRefGoogle ScholarPubMed
Adler, J. & Templeton, B. (1963). The amount of galactose genetic material in λ dg bacteriophage of different densities. J. molec. Biol. 7, 710720.CrossRefGoogle ScholarPubMed
Buttin, G. (1963 a). La biosynthèse induite de la galactokinase et l'induction simultanée de la séquence enzymatique. J. molec. Biol. 7, 164182.CrossRefGoogle Scholar
Buttin, G. (1963 b). Le déterminisme genétique de la regulation du metabolisme du galactose. J. molec. Biol. 7, 183205.Google Scholar
Campbell, A. M. (1962). Episomes. Adv. Genet. 11, 101145.CrossRefGoogle Scholar
Cohen, B. B. & Bishop, J. O. (1966). Purification of argininosuccinase from Neurospora and comparison of some properties of the wild-type enzyme and an enzyme purified by interallelic complementation. Genet. Res. 8, 243252.CrossRefGoogle Scholar
Davis, J. E. & Sinsheimer, R. L., (1963). The replication of bacteriophage MS2. I. Transfer of parental nucleic acid to progeny phage. J. molec. Biol. 6, 203207.Google Scholar
Echols, H., Reznichek, J. & Adhya, S. (1963). Complementation, recombination and suppression in galactose negative mutants of E. coli. Proc. natn. Acad. Sci. U.S.A. 50, 286.Google Scholar
Kalckar, H. M., Kurahashi, K. & Jordan, E. (1959). Hereditary defects in galactose metabolism in E. coli mutants. I. Determination of enzyme activities. Proc. natn. Acad. Sci. U.S.A. 45, 17761785.Google Scholar
Kurahashi, K. (1957). Enzyme formation in galactose negative mutants of Escherichia coli. Science, N.Y. 125, 114115.Google Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L., & Randal, R. J. (1951). Protein measurement with the Folin phenol reagent. J. biol. Chem. 193, 265275.Google Scholar
Morse, M. L. (1962). Preliminary genetic map of seventeen galactose mutants in E. coli K12. Proc. natn. Acad. Sci. U.S.A. 48, 13141318.Google Scholar
Paladini, A. C. & Leloir, L. F. (1952). Studies on uridine diphosphate glucose. Biochem. J. 51, 426430.Google Scholar
Signer, E. R. & Beckwith, J. R. (1966). The mechanism of attachment of bacteriophage φ 80 to the bacterial chromosome. J. molec. Biol. 22, 3351.Google Scholar
Soffer, R. L. (1961). Enzymatic expression of genetic units of function concerned with galactose metabolism in Escherichia coli. J. Bact. 82, 471478.CrossRefGoogle ScholarPubMed