Purification and amino acid sequence of a bacteriocin produced by Free

Abstract

A bacteriocin produced by has been purified to homogeneity by a rapid and simple four-step purification procedure which includes ammonium sulphate precipitation, chromatography with a cation-exchanger and Octyl Sepharose, and reverse-phase chromatography. The purification resulted in an approximately 80000-fold increase in the specific activity and about a 6-fold increase in the total activity. The amino acid composition and sequencing data indicated that the bacteriocin contained 43–44 amino acid residues. The predicted and isoelectric point of the bacteriocin are about 4600 and 8.6, respectively. Comparing the amino acid sequence of this bacteriocin with the sequences of leucocin A-UAL 187, sakacin P and curvacin A (bacteriocins produced by and , respectively) revealed that all four bacteriocins had in their N-terminal region the sequence Tyr-Gly-Asn-Gly-Val-Xaa-Cys, indicating that this concensus sequence is of fundamental importance for this group of bacteriocins. The bacteriocin from and sakacin P were very similar, having at least 25 common amino acid residues. The sequence similarity was greatest in the N-terminal half of the molecules – 17 of the first 19 residues were common – indicating the fundamental importance of this region. Leucocin A-UAL 187 and curvacin A had, respectively, at least 16 and 13 amino acid residues in common with the bacteriocin from .

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1992-09-01
2024-03-28
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References

  1. van Belkum M. J., Hayema B. J., Geis A., Kok J., Venema G. 1989; Cloning of two bacteriocin genes from a lactococcal bacteriocin plasmid. Applied and Environmental Microbiology 55:1187–1191
    [Google Scholar]
  2. van Belkum M. J., Hayema B. J., Jeeninga R. E., Kok J., Venema G. 1991a; Organization and nucleotide sequences of two lactococcal bacteriocin operons. Applied and Environmental Microbiology 57:492–498
    [Google Scholar]
  3. van Belkum M. J., Kok J., Venema G., Holo H., Nes I. F., Konings W. N., Abee T. 1991b; The bacteriocin lactococcin A specifically increases the permeability of lactococcal cytoplasmic membranes in a voltage-independent, protein mediated manner. Journal of Bacteriology 173:7934–7941
    [Google Scholar]
  4. Bhunia A. K., Johnson M. C., Ray B. 1988; Purification, characterization and antimicrobial spectrum of a bacteriocin produced by Pediococcus acidilactici. Journal of Applied Bacteriology 65:261–268
    [Google Scholar]
  5. Buchman G. W., Banerjee S., Hansen J. N. 1988; Structure, expression, and evolution of a gene encoding the precursor of nisin, a small protein antibiotic. Journal of Biological Chemistry 263:16260–16266
    [Google Scholar]
  6. Cornwell G. G., Sletten K., Johansson B., Westemark P. 1988; Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin. Biochemical and Biophysical Research Communications 154:648–653
    [Google Scholar]
  7. Daeschel M. A., Klaenhammer T. R. 1985; Association of a 13.6-megadalton plasmid in Pediococcus pentosaceus with bacteriocin activity. Applied and Environmental Microbiology 50:1538–1541
    [Google Scholar]
  8. Dodd H. M., Horn N., Gasson M. J. 1990; Analysis of the genetic determinant for production of the peptide antibiotic nisin. Journal of General Microbiology 136:555–566
    [Google Scholar]
  9. Fykse E.-M., Sletten K., Husby G., Cornwell G. G. 1988; The primary structure of the variable region of an immunoglobulin IV light-chain amyloid-fibril protein (AL GIL). Biochemical Journal 256:973–980
    [Google Scholar]
  10. Geis A., Jasjit J., Teuber M. 1983; Potential of lactic streptococci to produce bacteriocin. Applied and Environmental Microbiology 45:205–211
    [Google Scholar]
  11. Gonzalez C. F., Kunka B. 1987; Plasmid-associated bacteriocin production and sucrose fermentation in Pediococcus acidilactici. Applied and Environmental Microbiology 53:2534–2538
    [Google Scholar]
  12. Gross E., Morell J. 1971; The structure of nisin. Journal of the American Chemical Society 93:4634–4635
    [Google Scholar]
  13. Hastings J. W., Sailer M., Johnson K., Roy K. L., Vederas J. C., Stiles M. 1991; Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum. Journal of Bacteriology 173:7491–7500
    [Google Scholar]
  14. Henderson J. T., Chopko A. L., van Wassenaar P. D. 1992; Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0. Archives of Biochemistry and Biophysics295 (in the Press)
    [Google Scholar]
  15. Holo H., Nilssen ø., Nes I. F. 1991; Lactococcin A, a new bacteriocin from Lactococcus lactis subsp. cremoris: isolation and characterization of the protein and its gene. Journal of Bacteriology 173:3879–3887
    [Google Scholar]
  16. Hurst A. 1981; Nisin. Advances in Applied Microbiology 27:85–123
    [Google Scholar]
  17. Joerger M. C., Klaenhammer T. R. 1990; Cloning, expression, and nucleotide sequence of the Lactobacillus helveticus 481 gene encoding the bacteriocin helveticin J. Journal of Bacteriology 172:6339–6347
    [Google Scholar]
  18. Kaletta C., Entlan K. D. 1989; Nisin, a peptide antibiotic: cloning and sequencing of the nisA gene and posttranslational processing of its peptide product. Journal of Bacteriology 171:1597–1601
    [Google Scholar]
  19. Klaenhammer T. R. 1988; Bacteriocins of lactic acid bacteria. Biochimie 70:337–349
    [Google Scholar]
  20. Mørtvedt C. I., Nissen-Meyer J., Nes I. F. 1991; Purification and amino acid sequence of lactocin S, a bacteriocin produced by Lactobacillus sake L45. Applied and Environmental Microbiology 57:1829–1834
    [Google Scholar]
  21. Muriana P. M., Klaenhammer T. R. 1991a; Cloning, phenotypic expression, and DNA sequence of the gene for lactacin F, an antimicrobial peptide produced by Lactobacillus spp. Journal of Bacteriology 173:1779–1788
    [Google Scholar]
  22. Muriana P. M., Klaenhammer T. R. 1991b; Purification and partial characterization of lactacin F, a bacteriocin produced by Lactobacillus acidophilus 11088. Applied and Environmental Microbiology 57:114–121
    [Google Scholar]
  23. Sahl H.-G., Kordel M., Benz R. 1987; Voltage-dependent depolarization of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin. Archives of Microbiology 149:120–124
    [Google Scholar]
  24. Sletten K., Husby G. 1974; The complete amino acid sequence of non-immunoglobulin amyloid protein AS in rheumatoid arthritis. European Journal of Biochemistry 41:117–125
    [Google Scholar]
  25. Tagg J. R., Dajani A. S., Wannamaker L. W. 1976; Bacteriocins of gram-positive bacteria. Bacteriological Reviews 40:722–756
    [Google Scholar]
  26. Tichaczek P. S., Nissen-Meyer J., Nes I. F., Vogel R. F., Hammes W. P. 1992; Characterization of the bacteriocins curvacin A and sakacin P produced by Lactobacillus curvatus LTH1174 and L. sake LTH673. Systematic and Applied Microbiology15 (in the Press)
    [Google Scholar]
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