1887

Abstract

Summary: A new method has been developed for measuring peptide transport in aminoacid auxotrophs of by following induction of -galactosidase. Appearance of the enzyme was determined after addition of inducer and peptides to amino-acid starved bacteria. For a given number of lysine equivalents, the rate and the extent of enzyme synthesis were the same for lysine and lysyl peptides; similar results were found for glycine and glycyl peptides. Saturation constants for peptide transport were determined from the exogenous peptide concentration that gave half maximal rates of enzyme synthesis. The saturation constants, studies with mutants defective in peptide transport, and detection of competition between peptides for uptake, all endorsed earlier conclusions from growth tests about the structural specificities for peptide transport. The new method is quicker, more sensitive and more informative than growth tests.

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/content/journal/micro/10.1099/00221287-98-2-485
1977-02-01
2021-10-22
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References

  1. Ames G.F. 1964; Uptake of amino acids by Salmonella typhimurium. Archives of Biochemistry and Biophysics 104:1–18
    [Google Scholar]
  2. Barak Z., Gilvarg C. 1975a; Peptide transport. In Biomembranes 7 pp. 167–218 Eisenberg H., Katchalski-Katzir E., Manson L.A. Edited by New York:: Plenum Press.;
    [Google Scholar]
  3. Barak Z., Gilvarg C. 1975b; Specialised peptide transport system in Escherichia coli. Journal of Bacteriology 122:1200–1207
    [Google Scholar]
  4. Barak Z., Sarid S., Katchalski E. 1973; Inhibition of protein biosynthesis in Escherichia coli B by tri-l-omithine. European Journal of Biochemistry 34:317–324
    [Google Scholar]
  5. Cascieri T., Mallette M.F. 1974; New method for study of peptide transport in bacteria. Applied Microbiology 27:457–463
    [Google Scholar]
  6. Cowell J.L. 1974; Energetics of glycylglycine transport in Escherichia coli. Journal of Bacteriology 120:139–146
    [Google Scholar]
  7. Davis B.D., Mingioli E.S. 1950; Mutants of Escherichia coli requiring methionine or vitamin B12. Journal of Bacteriology 60:17–28
    [Google Scholar]
  8. Gilvarg C., Levin Y. 1972; Response of Escherichia coli to ornithyl peptides. Journal of Biological Chemistry 247:543–549
    [Google Scholar]
  9. Hayman S., Gatmaitan J.S., Patterson E.K. 1974; The relationship of extrinsic and intrinsic metal ions to the specificity of a dipeptidase from Escherichia coli b. Biochemistry; New York: 134486–4494
    [Google Scholar]
  10. Kessel D., Lubin M. 1963; On the distinction between peptidase activity and peptide transport. Biochimica et biophysica acta 71:656–663
    [Google Scholar]
  11. Lazdunski C., Basuttil J., Lazdunski A. 1975; Purification and properties of a periplasmic aminoendopeptidase from Escherichia coli. European Journal of Biochemistry 60:363–369
    [Google Scholar]
  12. Naider F., Becker J.M. 1975; Multiplicity of oligopeptide transport systems in Escherichia coli. Journal of Bacteriology 122:1208–1215
    [Google Scholar]
  13. Patterson E.K., Gatmaitan J.S., Hayman S. 1975; The effects of Mn2+ and Co2+ on the activities of a zinc metallodipeptidase from a mouse ascites tumor. Biochemistry; New York: 144261–4266
    [Google Scholar]
  14. Payne J.W. 1968; Oligopeptide transport in Escherichia coli: specificity with respect to side chain and distinction from dipeptide transport. Journal of Biological Chemistry 243:3395–3403
    [Google Scholar]
  15. Payne J.W. 1972a; The characterization of dipeptidases from Escherichia coli. Journal of General Microbiology 71:267–279
    [Google Scholar]
  16. Payne J.W. 1972b; Variations in the peptidase activities of Escherichia coli in response to environmental changes. Journal of General Microbiology 71:281–291
    [Google Scholar]
  17. Payne J.W. 1974; Peptide transport in Escherichia coli: permease specificity towards terminal amino group substituents. Journal of General Microbiology 80:269–276
    [Google Scholar]
  18. Payne J.W. 1975; Peptide transport in microorganisms. In Peptide Transport in Protein Nutrition pp. 283–365 Matthews D.M., Payne J.W. Edited by Amsterdam:: North Holland.;
    [Google Scholar]
  19. Payne J.W. 1976; Peptides and microorganisms. Advances in Microbial Physiology 13:55–113
    [Google Scholar]
  20. Payne J.W., Gilvarg C. 1971; Peptide transport. Advances in Enzymology 35:187–244
    [Google Scholar]
  21. Putnam S.L., Koch A.L. 1975; Complications in the simplest cellular enzyme assay: lysis of Escherichia coli for the assay of β-galactosidase. Analytical Biochemistry 63:350–360
    [Google Scholar]
  22. Simmonds S. 1970; Peptidase activity and peptide metabolism in Escherichia coli K-12. Biochemistry; New York: 91–9
    [Google Scholar]
  23. Simmonds S. 1972; Peptidase activity and peptide metabolism. In Peptide Transport in Bacteria and Mammalian Gut CIBA Foundation Symposium pp. 43–53 Amsterdam:: Associated Scientific Publishers.;
    [Google Scholar]
  24. Simmonds S., Szeto K.S., Fletterick C.G. 1976; Soluble tri- and dipeptidases in Escherichia coli k-12. Biochemistry; New York: 15261–271
    [Google Scholar]
  25. Sussman A.J., Gilvarg C. 1970; Peptidases in Escherichia coli k-12 capable of cleaving lysine homopeptides. Journal of Biological Chemistry 245:6518–6524
    [Google Scholar]
  26. Sussman A.J., Gilvarg C. 1971; Peptide transport and metabolism in bacteria. Annual Review of Biochemistry 40:397–408
    [Google Scholar]
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