Skip to main content
PMC home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1994 May;60(5):1652–1657. doi: 10.1128/aem.60.5.1652-1657.1994

Cloning, expression, and nucleotide sequence of genes involved in production of lactococcin DR, a bacteriocin from lactococcus lactis subsp. lactis.

A Rince 1, A Dufour 1, S Le Pogam 1, D Thuault 1, C M Bourgeois 1, J P Le Pennec 1
PMCID: PMC201532  PMID: 8017945

Abstract

The partial nucleotide sequence of a Lactococcus lactis subsp. lactis ADRIA 85LO30 bacteriocin-producing operon was determined. The first two open reading frames of the operon are necessary to get bacteriocin expression in L. lactis IL1403R.

Full text

PDF
1656

Images in this article

1656Image
on p.1656

Selected References

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

  1. De Graaf F. K., Oudega B. Production and release of cloacin DF13 and related colicins. Curr Top Microbiol Immunol. 1986;125:183–205. doi: 10.1007/978-3-642-71251-7_11. [DOI] [PubMed] [Google Scholar]
  2. Dufour A., Thuault D., Boulliou A., Bourgeois C. M., Le Pennec J. P. Plasmid-encoded determinants for bacteriocin production and immunity in a Lactococcus lactis strain and purification of the inhibitory peptide. J Gen Microbiol. 1991 Oct;137(10):2423–2429. doi: 10.1099/00221287-137-10-2423. [DOI] [PubMed] [Google Scholar]
  3. Engelke G., Gutowski-Eckel Z., Hammelmann M., Entian K. D. Biosynthesis of the lantibiotic nisin: genomic organization and membrane localization of the NisB protein. Appl Environ Microbiol. 1992 Nov;58(11):3730–3743. doi: 10.1128/aem.58.11.3730-3743.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Gilmore M. S., Segarra R. A., Booth M. C. An HlyB-type function is required for expression of the Enterococcus faecalis hemolysin/bacteriocin. Infect Immun. 1990 Dec;58(12):3914–3923. doi: 10.1128/iai.58.12.3914-3923.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Higgins C. F., Hiles I. D., Salmond G. P., Gill D. R., Downie J. A., Evans I. J., Holland I. B., Gray L., Buckel S. D., Bell A. W. A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria. Nature. 1986 Oct 2;323(6087):448–450. doi: 10.1038/323448a0. [DOI] [PubMed] [Google Scholar]
  6. Holo H., Nilssen O., Nes I. F. Lactococcin A, a new bacteriocin from Lactococcus lactis subsp. cremoris: isolation and characterization of the protein and its gene. J Bacteriol. 1991 Jun;173(12):3879–3887. doi: 10.1128/jb.173.12.3879-3887.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hynes W. L., Ferretti J. J., Tagg J. R. Cloning of the gene encoding Streptococcin A-FF22, a novel lantibiotic produced by Streptococcus pyogenes, and determination of its nucleotide sequence. Appl Environ Microbiol. 1993 Jun;59(6):1969–1971. doi: 10.1128/aem.59.6.1969-1971.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Juranka P., Zhang F., Kulpa J., Endicott J., Blight M., Holland I. B., Ling V. Characterization of the hemolysin transporter, HlyB, using an epitope insertion. J Biol Chem. 1992 Feb 25;267(6):3764–3770. [PubMed] [Google Scholar]
  9. Karn J., Matthes H. W., Gait M. J., Brenner S. A new selective phage cloning vector, lambda 2001, with sites for XbaI, BamHI, HindIII, EcoRI, SstI and XhoI. Gene. 1984 Dec;32(1-2):217–224. doi: 10.1016/0378-1119(84)90049-0. [DOI] [PubMed] [Google Scholar]
  10. Klaenhammer T. R. Bacteriocins of lactic acid bacteria. Biochimie. 1988 Mar;70(3):337–349. doi: 10.1016/0300-9084(88)90206-4. [DOI] [PubMed] [Google Scholar]
  11. Klein C., Kaletta C., Schnell N., Entian K. D. Analysis of genes involved in biosynthesis of the lantibiotic subtilin. Appl Environ Microbiol. 1992 Jan;58(1):132–142. doi: 10.1128/aem.58.1.132-142.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Piard J. C., Kuipers O. P., Rollema H. S., Desmazeaud M. J., de Vos W. M. Structure, organization, and expression of the lct gene for lacticin 481, a novel lantibiotic produced by Lactococcus lactis. J Biol Chem. 1993 Aug 5;268(22):16361–16368. [PubMed] [Google Scholar]
  13. Piard J. C., Muriana P. M., Desmazeaud M. J., Klaenhammer T. R. Purification and Partial Characterization of Lacticin 481, a Lanthionine-Containing Bacteriocin Produced by Lactococcus lactis subsp. lactis CNRZ 481. Appl Environ Microbiol. 1992 Jan;58(1):279–284. doi: 10.1128/aem.58.1.279-284.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Simon D., Chopin A. Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis. Biochimie. 1988 Apr;70(4):559–566. doi: 10.1016/0300-9084(88)90093-4. [DOI] [PubMed] [Google Scholar]
  16. Stoddard G. W., Petzel J. P., van Belkum M. J., Kok J., McKay L. L. Molecular analyses of the lactococcin A gene cluster from Lactococcus lactis subsp. lactis biovar diacetylactis WM4. Appl Environ Microbiol. 1992 Jun;58(6):1952–1961. doi: 10.1128/aem.58.6.1952-1961.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Tagg J. R., Dajani A. S., Wannamaker L. W. Bacteriocins of gram-positive bacteria. Bacteriol Rev. 1976 Sep;40(3):722–756. doi: 10.1128/br.40.3.722-756.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Thuault D., Beliard E., Le Guern J., Bourgeois C. M. Inhibition of Clostridium tyrobutyricum by bacteriocin-like substances produced by lactic acid bacteria. J Dairy Sci. 1991 Apr;74(4):1145–1150. doi: 10.3168/jds.S0022-0302(91)78266-0. [DOI] [PubMed] [Google Scholar]
  19. van Belkum M. J., Hayema B. J., Jeeninga R. E., Kok J., Venema G. Organization and nucleotide sequences of two lactococcal bacteriocin operons. Appl Environ Microbiol. 1991 Feb;57(2):492–498. doi: 10.1128/aem.57.2.492-498.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES