1887

Microbiology Society logo

Volume 140, Issue 3

Cloning, sequencing and characterization of the gene encoding a proline iminopeptidase from subsp. CNRZ 397 Free

Abstract

The proline iminopeptidase (PepIP) of subsp. is a major peptidase located in the cell envelope. Its structural gene () has been cloned into pUC18 and expressed at a very high level in to give a IP activity 15000-fold higher than that found in subsp. . The nucleotide sequence of the gene revealed an open reading frame of 295 codons encoding a protein with a predicted of 33006, which is consistent with the apparent size of the gene product. The amino acid sequence of PepIP shows significant homology with those of other hydrolases involved in the degradation of cyclic compounds. In particular, there is a region which includes an identified catalytic site containing a serine residue and a motif specific for the active sites of prolyloligopeptidases (Gly-X-Ser-X-Gly-Gly). The PepIP opens a new way for supplying cells with proline using the peptides resulting from the proteolytic degradation of caseins.

  • Received:
  • Accepted:
  • Revised:
  • Published Online:
Keyword(s): casein hydrolysis , Lactobacillus delbrueckii subsp. bulgaricus , proline iminopeptidase and prolyl oligopeptidases
© Society for General Microbiology 1994
Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-140-3-527
1994-03-01
2024-04-16
Loading full text...

Full text loading...

/deliver/fulltext/micro/140/3/mic-140-3-527.html?itemId=/content/journal/micro/10.1099/00221287-140-3-527&mimeType=html&fmt=ahah

References

  1. Adler H., Fisher W., Cohen H., Hardigree A. Miniature Escherichia coli cells deficient in DNA. Proc Natl Acad Sci USA (1967); 57:321–326
     [Google Scholar]
  2. Atlan D., Laloi P., Portalier R. Isolation and characterization of aminopeptidase-deficient Lactobacillus bulgaricus mutants. Appl Environ Microbiol (1989); 55:1717–1723
     [Google Scholar]
  3. Atlan D., Laloi P., Portalier R. X-proline-dipeptidyl-aminopeptidase of Lactobacillus delbrueckii subsp. bulgaricus: characterization of the enzyme and isolation of deficient mutants. Appl Environ Microbiol (1990); 56:2174–2179
     [Google Scholar]
  4. Blanc B., Laloi P., Atlan D., Gilbert C., Portalier R. Two cell wall-associated aminopeptidases from Lactobacillus helveticus and the purification and characterization of APII from strain ITGL1. J Gen Microbiol (1993); 139:1441–1448
     [Google Scholar]
  5. Casey M.G., Meyer J. Presence of X-prolyl-dipeptidyl-peptidase in lactic acid bacteria. J Dairy Sci (1985); 68:3212–3215
     [Google Scholar]
  6. Dessen P., Fondrat C., Valancien C., Mugnier C. Bisance: a French service for access to biomolecular sequence databases. CABIOS (1990); 6:335–336
     [Google Scholar]
  7. Falany G., McQuiddy P., Kasper B. Structure and organization of the microsomal xenobiotic epoxide hydrolase gene. J Biol Chem (1987); 262:5924–5930
     [Google Scholar]
  8. Gilbert C., Atlan D., Blanc B., Portalier R. Proline iminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397: purification and characterization. Microbiology (1994); 140:537–542
     [Google Scholar]
  9. Hayase N., Taira K., Furukawa K. Pseudomonas putida KF715 bphABCD operon encoding biphenyl and polychlorinated biphenyl degradation: cloning, analysis and expression in soil bacteria. J Bacteriol (1990); 172:1160–1164
     [Google Scholar]
  10. Hessing J. The primary structure of atropinesterase from Pseudomonas putida (1983) PhD thesis, University of Leiden, The Netherlands;
     [Google Scholar]
  11. Hickey M.W., Hillier A.J., Jago G.R. Peptidase activities in lactobacilli. Austr J Dairy Technol (1983); 9:118–123
     [Google Scholar]
  12. Higgins D., Sharp P. clustal: a package for multiple sequence alignment on a microcomputer. Gene (1988); 73:237–244
     [Google Scholar]
  13. Horn J., Harayama S., Timmis K. DNA sequence determination of the TOL plasmid (PWWO) xylGFJ genes of Pseudomonas putida: implications for the evolution of aromatic catabolism. Mol Microbiol (1991); 5:2459–2474
     [Google Scholar]
  14. Hottinger H., Ohgi T., Zwahlen M., C, Dhamija S., Söll D. Allele-specific complementation of an Escherichia coli leuB mutation by a Lactobacillus bulgaricus tRNA gene. Gene (1987); 60:75–83
     [Google Scholar]
  15. Kanatani A., Masuda T., Shimoda T., Misoka F., Lin X., Yoshimoto T., Tsuru D. Protease II from Escherichia coli: sequencing and expression of the enzyme gene and characterization of the expressed enzyme. J Biochem (1991); 110:315–320
     [Google Scholar]
  16. Khalid N.M., Marth E.H. Purification and partial characterization of a prolyl-dipeptidyl aminopeptidase from Lactobacillus helveticus CNRZ32. Appl Environ Microbiol (1990); 56:381–388
     [Google Scholar]
  17. Kitazano A., Yoshimoto T., Tsuru D. Cloning, sequencing, and high expression of the proline iminopeptidase gene from Bacillus coagulans. J Bacteriol (1992); 174:7919–7925
     [Google Scholar]
  18. Kiwaki M., Ikemura H., Shimizu-Kadota M., Hirashima A. Molecular characterization of a cell wall-associated proteinase gene from Streptococcus lactis NCD0763. Mol Microbiol (1989); 3:359–369
     [Google Scholar]
  19. Kok J. Genetics of the proteolytic system of lactic acid bacteria. FEMS Microbiol Rev (1990); 87:15–42
     [Google Scholar]
  20. Kyte J., Doolittle R. A simple method for displaying the hydropathic character of a protein. J Mol Biol (1982); 157:105–132
     [Google Scholar]
  21. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (1970); 221:680–685
     [Google Scholar]
  22. Laloi P., Atlan D., Blanc B., Gilbert G., Portalier R. Cell-wall associated proteinase of Eactobacillus delbrueckii subsp. bulgaricus CNRZ397: Differential extraction, purification and properties of the enzyme. Appl Microbiol Biotechnol (1991); 36:196–204
     [Google Scholar]
  23. Langella P., Chopin A. Effect of restriction-modification systems on transfer of foreign DNA into Lactococcus lactis subsp. lactis. FEMS Microbiol Lett (1989); 59:301–306
     [Google Scholar]
  24. Lazzaroni J.C., Portalier R. The excC gene of Escherichia coli K-12 required for the cell envelope integrity encodes the peptidoglycan-associated lipoprotein (PAL). Mol Microbiol (1992); 6:735–742
     [Google Scholar]
  25. Lazzaroni J.C., Fognini-Lefebvre N., Portalier R. Cloning of the excC and excD genes involved in the release of periplasmic proteins by Escherica coli K-12. Mol & Gen Genet (1989); 218:460–464
     [Google Scholar]
  26. Lipman D., Pearson W. Improved tools for biological sequence comparison. Proc. Natl Acad Sci USA (1988); 85:2444–2448
     [Google Scholar]
  27. Makinen K.K. The proline iminopeptidases of the human oral cavity. Partial purification and characterization. . Acta Chem Scand (1969); 23:1409–1438
     [Google Scholar]
  28. de Man J.C., Rogosa M., Sharpe M.E. A medium for the cultivation of lactobacilli. J Appl Bacteriol (1960); 23:130–135
     [Google Scholar]
  29. Meyer J., Jordi R. Purification and characterization of X-prolyl-dipeptidyl-aminopeptidase from Lactobacillus lactis and from Streptococcus thermophilus. J Dairy Sci (1987); 70:738–745
     [Google Scholar]
  30. Miller J. Experiments in Molecular Genetics (1972) Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
     [Google Scholar]
  31. Myakawa H., Kobayashi S., Shimamura S., Tomita M. Purification and characterization of an aminopeptidase from Lactobacillus helveticus LHE-511. J Dairy Sci (1992); 75:27–35
     [Google Scholar]
  32. Nordlund I., Shingler V. Nucleotide sequences of the meta-cleavage pathway enzymes 2-hydroxymuconic semialdehyde deshydrogenase and 2,2-hydroxymuconic semialdehyde hydrolase from Pseudomonas CF600. Biochim Biophys Acta (1990); 1049:227–230
     [Google Scholar]
  33. Rawlings N.D., Polgar L., Barrett A.J. A new family of serine-type peptidases related to prolyl oligopeptidase. Biochem J (1991); 279:907–911
     [Google Scholar]
  34. Rennex D., Hemmings B., Hofsteenge J., Stone S. cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue. Biochemistry (1991); 30:2195–2203
     [Google Scholar]
  35. Rodriguez R.L., Tait R.C. Recombinant DNA Techniques: an Introduction (1983) New York: Addison-Wesley; pp 194–196
     [Google Scholar]
  36. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: A Laboratory Manual. (1989) Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
     [Google Scholar]
  37. Sanger F., Nicklen S., Coulson A. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA (1977); 74:5463–5467
     [Google Scholar]
  38. Sarid S., Berger A., Katchalski E. Proline iminopeptidase. II. Purification and comparison with iminodipeptidase. J Biol Chem (1962); 237:2207–2212
     [Google Scholar]
  39. Schmidt B., Adams R., Requardt C., Power S., Mainzer S. Expression and nucleotide sequence of the Lactobacillus bulgaricus β-galactosidase gene cloned in Escherichia colt. J Bacteriol (1989); 171:625–635
     [Google Scholar]
  40. Simon D., Chopin A. Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis. Biochimie (1988); 70:559–566
     [Google Scholar]
  41. Skoda R., Demierre A., McBride O., Gonzales F., Meyer U. Human microsomal xenobiotic epoxide hydrolase. J Biol Chem (1988); 263:1549–1554
     [Google Scholar]
  42. Smid E.J., Konings W. Relationship between utilization of proline and proline-containing peptides and growth of Lactococcus lactis. J Bacteriol (1990); 172:5286–5292
     [Google Scholar]
  43. Smid E.J., Poolman B., Konings W. Casein utilization by lactococci. Appl Environ Microbiol (1991); 57:2447–2452
     [Google Scholar]
  44. Terzaghi B.E., Sandine W.E. Improved medium for lactic streptococci and their bacteriophages. Appl Environ Microbiol (1975); 29:807–813
     [Google Scholar]
  45. Van Alen-Boerrigter I., Baankreis R., De Vos W. Characterization and overexpression of the Lactococcus lactis pepN gene and localization of its product, aminopeptidase N. Appl Environ Microbiol (1991); 57:2555–2561
     [Google Scholar]
  46. Webster R. The tol gene products and the import of macromolecules into Escherichia coli. Mol Microbiol (1991); 5:1005–1011
     [Google Scholar]
  47. Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene (1985); 33:103–119
     [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-140-3-527
Loading
Cloning, sequencing and characterization of the pepIP gene encoding a proline iminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397
Microbiology 140, 527 (1994); https://doi.org/10.1099/00221287-140-3-527
/content/journal/micro/10.1099/00221287-140-3-527
/content/journal/micro/10.1099/00221287-140-3-527
Loading

Data & Media loading...

Most cited Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error