Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1982 Nov;152(2):848–854. doi: 10.1128/jb.152.2.848-854.1982

Genetics and regulation of peptidase N in Escherichia coli K-12.

M T McCaman, A McPartland, M R Villarejo
PMCID: PMC221539  PMID: 6752120

Abstract

Escherichia coli K-12 strains contain a cytoplasmic activity, peptidase N, capable of hydrolyzing alanine-p-nitroanilide. Mutations in the structural gene for the enzyme, pepN, were mapped, and the properties of mutant strains were examined. The pepN locus lay between ompF and asnS at approximately 20.8 min on the E. coli chromosome. Loss of peptidase N activity through mutation had no apparent effect on the growth rate or nutritional needs of the cell. Enzyme levels in wild-type strains were constant throughout the growth cycle and were constitutive in all of the growth media tested. Starvation for carbon, nitrogen, or phosphate also did not alter enzyme levels. Constitutive expression of peptidase N is consistent with the idea that the enzyme plays a significant role in the degradation of intracellularly generated peptides.

Full text

PDF
854

Selected References

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

  1. Bachmann B. J., Low K. B. Linkage map of Escherichia coli K-12, edition 6. Microbiol Rev. 1980 Mar;44(1):1–56. doi: 10.1128/mr.44.1.1-56.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Casadaban M. J., Cohen S. N. Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: in vivo probe for transcriptional control sequences. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4530–4533. doi: 10.1073/pnas.76.9.4530. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Goldberg A. L., Dice J. F. Intracellular protein degradation in mammalian and bacterial cells. Annu Rev Biochem. 1974;43(0):835–869. doi: 10.1146/annurev.bi.43.070174.004155. [DOI] [PubMed] [Google Scholar]
  4. HORIUCHI T., TOMIZAWA J. I., NOVICK A. Isolation and properties of bacteria capable of high rates of beta-galactosidase synthesis. Biochim Biophys Acta. 1962 Jan 22;55:152–163. doi: 10.1016/0006-3002(62)90941-1. [DOI] [PubMed] [Google Scholar]
  5. Inouye M., Halegoua S. Secretion and membrane localization of proteins in Escherichia coli. CRC Crit Rev Biochem. 1980;7(4):339–371. doi: 10.3109/10409238009105465. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  8. 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]
  9. 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]
  10. 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]
  11. Low K. B. Escherichia coli K-12 F-prime factors, old and new. Bacteriol Rev. 1972 Dec;36(4):587–607. doi: 10.1128/br.36.4.587-607.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. McCaman M. T., Villarejo M. R. Structured and catalytic properties of peptidase N from Escherichia coli K-12. Arch Biochem Biophys. 1982 Feb;213(2):384–394. doi: 10.1016/0003-9861(82)90564-1. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Miller C. G., Green L. Degradation of abnormal proteins in peptidase-deficient mutants of Salmonella typhimurium. J Bacteriol. 1981 Sep;147(3):925–930. doi: 10.1128/jb.147.3.925-930.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. 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]
  16. 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]
  17. Miller C. G., Schwartz G. Peptidase-deficient mutants of Escherichia coli. J Bacteriol. 1978 Aug;135(2):603–611. doi: 10.1128/jb.135.2.603-611.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Miller C. G., Zipser D. Degradation of Escherichia coli beta-galactosidase fragments in protease-deficient mutants of Salmonella typhimurium. J Bacteriol. 1977 Apr;130(1):347–353. doi: 10.1128/jb.130.1.347-353.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Murgier M., Pelissier C., Lazdunski A., Lazdunski C. Existence, localization and regulation of the biosynthesis of aminoendopeptidase in gram-negative bacteria. Eur J Biochem. 1976 Jun 1;65(2):517–520. doi: 10.1111/j.1432-1033.1976.tb10368.x. [DOI] [PubMed] [Google Scholar]
  20. Ratzkin B., Roth J. Cluster of genes controlling proline degradation in Salmonella typhimurium. J Bacteriol. 1978 Feb;133(2):744–754. doi: 10.1128/jb.133.2.744-754.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Semple K. S., Silbert D. F. Mapping of the fabD locus for fatty acid biosynthesis in Escherichia coli. J Bacteriol. 1975 Mar;121(3):1036–1046. doi: 10.1128/jb.121.3.1036-1046.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. 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]
  23. Tommassen J., Lugtenberg B. Outer membrane protein e of Escherichia coli K-12 is co-regulated with alkaline phosphatase. J Bacteriol. 1980 Jul;143(1):151–157. doi: 10.1128/jb.143.1.151-157.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. 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]
  25. Yen C., Green L., Miller C. G. Degradation of intracellular protein in Salmonella typhimurium peptidase mutants. J Mol Biol. 1980 Oct 15;143(1):21–33. doi: 10.1016/0022-2836(80)90122-9. [DOI] [PubMed] [Google Scholar]
  26. Yen C., Green L., Miller C. G. Peptide accumulation during growth of peptidase deficient mutants. J Mol Biol. 1980 Oct 15;143(1):35–48. doi: 10.1016/0022-2836(80)90123-0. [DOI] [PubMed] [Google Scholar]

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

RESOURCES