Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1978 Aug;135(2):603–611. doi: 10.1128/jb.135.2.603-611.1978

Peptidase-deficient mutants of Escherichia coli.

C G Miller, G Schwartz
PMCID: PMC222421  PMID: 355237

Abstract

Mutant derivatives of Escherichia coli K-12 deficient in several peptidases have been obtained. Mutants lacking a naphthylamidase, peptidase N, were isolated by screening for colonies unable to hydrolyze L-alanine beta-naphthylamide. Other mutants were isolated using positive selections for resistance to valine peptides. Mutants lacking peptidase A, a broad-specificity aminopeptidase, were obtained by selection for resistance to L-valyl-L-leucine amide. Mutants lacking a dipeptidase, peptidase D, were isolated from a pepN pepA strain by selection for resistance to L-valyl-glycine. Starting with a pepN pepA pepD strain, selection for resistance to L-valyl-glycyl-glycine or several other valine peptides produced mutants deficient in another aminopeptidase, peptidase B. Mutants resistant to L-valyl-L-proline lack peptidase Q, an activity capable of rapid hydrolysis of X-proline dipeptides. Using these selection procedures, a strain (CM89) lacking five different peptidases has been isolated. Although still sensitive to valine, this strain is resistant to a variety of valine di- and tripeptides. The ability of this strain to use peptides as sources of amino acids is much more restricted than that of wild-type E. coli strains. Strains containing only one of the five peptidases missing in CM89 have been constructed by transduction. The peptide utilization profiles of these strains show that each of the five peptidases can function during growth in the catabolism of peptides.

Full text

PDF
603

Images in this article

605Image
on p.605
607Image
on p.607
608Image
on p.608

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barak Z., Gilbarg C. Specialized peptide transport system in Escherichia coli. J Bacteriol. 1975 Jun;122(3):1200–1207. doi: 10.1128/jb.122.3.1200-1207.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Brown J. L. Purification and properties of dipeptidase M from Escherichia coli B. J Biol Chem. 1973 Jan 25;248(2):409–416. [PubMed] [Google Scholar]
  3. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  4. De Felice M., Guardiola J., Lamberti A., Iaccarino M. Escherichia coli K-12 mutants altered in the transport systems for oligo- and dipeptides. J Bacteriol. 1973 Nov;116(2):751–756. doi: 10.1128/jb.116.2.751-756.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. KESSEL D., LUBIN M. On the distinction between peptidase activity and peptide transport. Biochim Biophys Acta. 1963 Jun 4;71:656–663. doi: 10.1016/0006-3002(63)91139-9. [DOI] [PubMed] [Google Scholar]
  6. Latil M., Murgier M., Lazdunski A., Lazdunski C. Isolation and genetic mapping of Escherichia coli aminopeptidase mutants. Mol Gen Genet. 1976 Oct 18;148(1):43–47. doi: 10.1007/BF00268544. [DOI] [PubMed] [Google Scholar]
  7. Lazdunski A., Murgier M., Lazdunski C. Evidence for an aminoendopeptidase localized near the cell surface of Escherichia coli. Regulation of synthesis by inorganic phosphate. Eur J Biochem. 1975 Dec 15;60(2):349–355. doi: 10.1111/j.1432-1033.1975.tb21009.x. [DOI] [PubMed] [Google Scholar]
  8. Lazdunski C., Busuttil J., Lazdunski A. Purification and properties of a periplasmic aminoendopeptidase from Escherichia coli. Eur J Biochem. 1975 Dec 15;60(2):363–369. doi: 10.1111/j.1432-1033.1975.tb21011.x. [DOI] [PubMed] [Google Scholar]
  9. Lewis W. H., Harris H. Human red cell peptidases. Nature. 1967 Jul 22;215(5099):351–355. doi: 10.1038/215351a0. [DOI] [PubMed] [Google Scholar]
  10. McHugh G. L., Miller C. G. Isolation and characterization of proline peptidase mutants of Salmonella typhimurium. J Bacteriol. 1974 Oct;120(1):364–371. doi: 10.1128/jb.120.1.364-371.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Miller C. G. Gentic mapping of Salmonella typhimurium peptidase mutations. J Bacteriol. 1975 Apr;122(1):171–176. doi: 10.1128/jb.122.1.171-176.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Miller C. G., Mackinnon K. Peptidase mutants of Salmonella typhimurium. J Bacteriol. 1974 Oct;120(1):355–363. doi: 10.1128/jb.120.1.355-363.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Miller C. G. Peptidases and proteases of Escherichia coli and Salmonella typhimurium. Annu Rev Microbiol. 1975;29:485–504. doi: 10.1146/annurev.mi.29.100175.002413. [DOI] [PubMed] [Google Scholar]
  14. Murgier M., Pelissier C., Lazdunski A. Aminopeptidase N from Escherichia coli. Unusual interactions with the cell surface. Eur J Biochem. 1977 Apr 15;74(3):425–433. doi: 10.1111/j.1432-1033.1977.tb11408.x. [DOI] [PubMed] [Google Scholar]
  15. Patterson E. K., Gatmaitan J. S., Hayman S. Substrate specificity and pH dependence of dipeptidases purified from Escherichia coli B and from mouse ascites tumor cells. Biochemistry. 1973 Sep 11;12(19):3701–3709. doi: 10.1021/bi00743a020. [DOI] [PubMed] [Google Scholar]
  16. Simmonds S., Szeto K. S., Fletterick C. G. Soluble tri- and dipeptidases in Escherichia coli K-12+. Biochemistry. 1976 Jan 27;15(2):261–271. doi: 10.1021/bi00647a004. [DOI] [PubMed] [Google Scholar]
  17. Sussman A. J., Gilvarg C. Peptidases in Escherichia coli K-12 capable of cleaving lysine homopeptides. J Biol Chem. 1970 Dec 25;245(24):6518–6524. [PubMed] [Google Scholar]
  18. Sussman A. J., Gilvarg C. Peptide transport and metabolism in bacteria. Annu Rev Biochem. 1971;40:397–408. doi: 10.1146/annurev.bi.40.070171.002145. [DOI] [PubMed] [Google Scholar]
  19. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  20. Vogt V. M. Purification and properties of an aminopeptidase from Escherichia coli. J Biol Chem. 1970 Sep 25;245(18):4760–4769. [PubMed] [Google Scholar]
  21. Yang L. M., Somerville R. L. Purification and properties of a new aminopeptidase from Escherichia COLI K12. Biochim Biophys Acta. 1976 Sep 14;445(2):406–419. doi: 10.1016/0005-2744(76)90094-2. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES