Previous Article | Next Article ![]()
Applied and Environmental Microbiology, December 2004, p. 7303-7310, Vol. 70, No. 12
0099-2240/04/$08.00+0 DOI: 10.1128/AEM.70.12.7303-7310.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Department of Chemistry, Biotechnology and Food Science, Agricultural University of Norway, Ås,1 Norwegian Dairies Association, Oslo, Norway2
Received 5 April 2004/ Accepted 30 July 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.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»