β-Galactosidase from Osmotic Remedial Lactose Utilization Mutants of E. Coli

  • R. T. Vinopal
  • S. A. Wartell
  • K. S. Kolowsky
Part of the Basic Life Sciences book series (BLSC, volume 14)


Retrieval of genetic information for synthesis of an enzyme is usually thought of in terms of transfer of sequence information — transcription of the base sequence of the gene into mRNA and translation of mRNA into the amino acid sequence of the polypeptide chain. The final expression of the gene, folding of the polypeptide to form the biologically active globular protein, is considered to result automatically from the sequence of amino acids. An information specialist will point out that the amino acid sequence does not possess enough information to specify the precisely folded shape of the active enzyme. The additional information comes from the specification of the environment in which the polypeptide folds. Anfinsen (1973) describes the thermodymanic hypothesis for protein folding in this way: “This hypothesis states that the three-dimensional structure of a native protein in its normal physiological milieu (solvent, pH, ionic strength, presence of other components such as metal ions or prosthetic groups, temperature, and other) is the one in which the Gibbs free energy of the whole system is the lowest; that is, that the native conformation is determined by the totality of interatomic interactions and hence by the amino acid sequence in a given environment. In terms of natural selection through the ‘design’ of macromolecule during evolution, this idea emphasizes the fact that a protein molecule only makes stable structural sense when it exist under conditions similar to those for which it was selected — the so-called physiological state.”


Compatible Solute Monovalent Cation Neurospora Crassa Osmotic Concentration Lactose Utilization 
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  1. Anfinsen, C. B., 1973, Principles that govern the folding of protein chains, Science, 181: 223.PubMedCrossRefGoogle Scholar
  2. Atkinson, D. E., 1969, Limitation of metabolic concentrations and the conservation of solvent capacity in the living cell, in: “Current Topics in Cellular Regulation,” Vol. I, B. L. Horecker and E. R. Stadtman, eds., Academic Press, Inc., New York.Google Scholar
  3. Bassel, J. and Douglas, H. C., 1970, Relationship between solute permeability and osmotic remediability in a galactose-negative strain of Saccharomyces cerevisiae, J. Bacteriol., 104: 707.PubMedGoogle Scholar
  4. Brown, A. D., 1976, Microbial water stress, Bacteriol. Rev., 40: 803.Google Scholar
  5. Bukhari, A. I. and Zipser, D., 1973, Mutants of Escherichia coli with a defect in the degradation of nonsense fragments, Nature New Biology, 243: 238.PubMedCrossRefGoogle Scholar
  6. Clark, D. J. and Maaloe, O., 1967, DNA replication and the division cycle in Escherichia coli, J. Mol. Biol., 23: 99.CrossRefGoogle Scholar
  7. Colb, M. and Shapiro, A., pH-conditional mutant of Escherichia coli, Proc. Natl. Acad. Sci. USA, 74: 5637.Google Scholar
  8. Fincham, J. R. S., and Baron, A. J., 1977, The molecular basis of an osmotically repairable mutant of Neurospora crassa producing unstable glutamate dehydrogenase, J. Mol. Biol., 110: 627.PubMedCrossRefGoogle Scholar
  9. Fluck, M. M., Salser, W., and Epstein, R. H., 1977, The influence of the reading context upon suppression of nonsense codons, Molec. Gen. Genet., 151: 137.CrossRefGoogle Scholar
  10. Goldberg, A. L. and St. John, A. C,,1976, Intracellular protein degradation in mammalian and bacterial cells: part 2, Ann. Rev. Biochem., 45: 747.Google Scholar
  11. Hawthorne, D. C. and Friis, J., 1964, Osmotic-remedial mutants. A riew classification for nutritional mutants in yeast, Genetics, 50: 829.PubMedGoogle Scholar
  12. Ingraham, J. L., 1973, Genetic regulation of temperature responses, in: “Temperature and Life,” Precht, Christopherson, Hensel, and Larcher, eds., Springer-Verlag, New York.Google Scholar
  13. Kohno, T. and Roth, J., 1979, Electrolyte effects on the activity of mutant enzymes in vivo and in vitro, Biochemistry, 18: 1386.PubMedCrossRefGoogle Scholar
  14. Laemli, U. K., 1970, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature (London), 227: 680.CrossRefGoogle Scholar
  15. Langridge, J., 1968, Thermal responses of mutant enzymes and temperature limits to growth, Molec. Gen. Genet., 103: 116.CrossRefGoogle Scholar
  16. Langridge, J., 1974, Mutation spectra and the neutrality of mutations, Aust. J. Biol, Sci., 27: 309.Google Scholar
  17. Langridge, J., 1974, Genetic and enzymatic experiments relating to the quaternary structure of g-galactosidase, Aust. J. Biol. Sci., 27: 321.PubMedGoogle Scholar
  18. Manley, J. L., 1978, Synthesis and degradation of termination and premature-termination fragments of β-galactosidase in vitro and in vivo, J. Mol. Biol., 125: 40.Google Scholar
  19. Martin, C. E. and DeBusk, A. G., 1975, Temperature-sensitive, osmotic remedial mutants of Neurospora crassa: osmotic pressure induced alterations of enzyme stability, Molec. Gen. Genet., 136: 31.CrossRefGoogle Scholar
  20. Measures, J. C., 1973, Role of amino acids in osmoregulation of non-halophilic bacteria, Nature (London), 257: 398.CrossRefGoogle Scholar
  21. Miller, J. H., 1972, “Experiments in Molecular Genetics,” Cold Spring Harbor Laboratory, New York.Google Scholar
  22. Roberts, G. A. and Charles, H. P., 1970, Mutants of Neurospora crassa, Salmonella typhimurium, and Escherichia coli specifically inhibited by carbon dioxide, J. Gen. Microbiol., 63: 21.PubMedGoogle Scholar
  23. Russell, R. R. B., 1972, Temperature-sensitive osmotic remedial mutants of Escherichia coli, J. Bacteriol., 112: 661.PubMedGoogle Scholar
  24. Schobert, B., 1977, Is there an osmotic regulatory mechanism in algae and higher plants ?, J. Theor. Biol., 68: 17.PubMedCrossRefGoogle Scholar
  25. Singh, A. and Sherman, F., 1975, Genetic and physiological characterization of met15 mutants of Saccharomyces cerevisiae; a selective system for forward and reverse mutations, Genetics, 81: 75.PubMedGoogle Scholar
  26. Truman, P. and Berquist, P. L., 1976, Genetic and biochemical characterization of some missence mutations in the lacZ gene of Escherichia coli K-12, J. Bacteriol., 126: 1063.PubMedGoogle Scholar
  27. Wallenfels, K. and Weil, R., 1972, 3-galactosidase, in: “The Enzymes,” Vol. 7, P. Boyer, ed., Academic Press, New York.Google Scholar
  28. Zengel, J. M., Young, R., Dennis, P. P., and Nomura, M., 1977, Role of ribosomal protein S12 in peptide chain elongation: analysis of pleiotropic, streptomycin-resistant mutants of Escherichia coli, J. Bacteriol., 129: 1320.PubMedGoogle Scholar
  29. Zimmerman, R. A., Garvin, R. T., and Gorini, L., 1971, Alteration of a 30S ribosomal protein accompanying the ram mutation in Escherichia coli, Proc. Natl. Acad. Sci. USA, 68: 2263.CrossRefGoogle Scholar
  30. Zipser, D., Zabell, S., Rothman, J., Grodzicker, T., Wenk, M., and Novitski, M., 1970, Fine structure of the gradient of polarity in the Z gene of the lac operon of Escherichia coli, J. Mol. Biol., 49: 251.PubMedCrossRefGoogle Scholar
  31. Zipser, D. and Bhavser, P., 1976, Missense mutations in the lacZ gene that result in degradation of g-galactosidase structural protein, J. Bacteriol., 127: 1538.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • R. T. Vinopal
    • 1
  • S. A. Wartell
    • 1
  • K. S. Kolowsky
    • 1
  1. 1.Microbiology Section, U-44 Biological Sciences GroupUniversity of ConnecticutStorrsUSA

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