Molecular and genetic characterization of propionicin F, a bacteriocin from Propionibacterium freudenreichii

• Published in: Applied and Environmental Microbiology 2004-12, Vol.70 (12), p.7303-7310
• Main Authors: Brede, D.A, Faye, T, Johnsborg, O, Odegard, I, Nes, I.F, Holo, H
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; amino acid sequences; Anti-Bacterial Agents - pharmacology; antibacterial properties; Bacteria; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; bacteriocins; Bacteriocins - chemistry; Bacteriocins - metabolism; Bacteriocins - pharmacology; Bacteriology; Base Sequence; Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; cheese starters; Fundamental and applied biological sciences. Psychology; gene expression; genes; Genetics; messenger RNA; Microbial Sensitivity Tests; Microbiology; Miscellaneous; Mission oriented research; Molecular biology; Molecular Sequence Data; nucleotide sequences; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains; pcfA gene; Physiology and Biotechnology; Propionibacterium - drug effects; Propionibacterium - genetics; Propionibacterium - metabolism; Propionibacterium freudenreichii; Sequence Analysis, DNA; transcription (genetics)
• ISSN: 0099-2240; 1098-5336
• DOI: 10.1128/AEM.70.12.7303-7310.2004

This work describes the purification and characterization of propionicin F, the first bacteriocin isolated from Propionibacterium freudenreichii. The bacteriocin has a bactericidal activity and is only active against strains of P. freudenreichii. Propionicin F appears to be formed through a processing pathway new to bacteriocins. The mass of the purified bacteriocin was determined by mass spectrometry, and the N-terminal amino acid sequence was determined by Edman degradation. Sequencing of pcfA, the bacteriocin structural gene, revealed that propionicin F corresponds to a 43-amino-acid peptide in the central part of a 255-amino-acid open reading frame, suggesting that mature propionicin F is excised from the probacteriocin by N- and C-terminal proteolytic modifications. DNA sequencing and Northern blot hybridizations revealed that pcfA is cotranscribed with genes encoding a putative proline peptidase and a protein from the radical S-adenosylmethionine family. A gene encoding an ABC transporter was also identified in close proximity to the bacteriocin structural gene. The potential role of these genes in propionicin F maturation and secretion is discussed.