Abstract:
: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.
journal_name
Appl Environ Microbioljournal_title
Applied and environmental microbiologyauthors
Brede DA,Faye T,Johnsborg O,Odegård I,Nes IF,Holo Hdoi
10.1128/AEM.70.12.7303-7310.2004keywords:
subject
Has Abstractpub_date
2004-12-01 00:00:00pages
7303-10issue
12eissn
0099-2240issn
1098-5336pii
70/12/7303journal_volume
70pub_type
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