Journal Article


C Hill
R P Ross
G Jung
H G Sahl
M Josten
R W Jack
M P Ryan



chromatography high pressure liquid lacticin 481 molecular sequence data amino acid sequence serine anti bacterial agents amino acid substitution mass spectrometry protein processing post translational isolation purification metabolism bacterial proteins bacteriocins chemistry alanine

Extensive post-translational modification, including serine to D-alanine conversion, in the two-component lantibiotic, lacticin 3147. (1999)

Abstract Lacticin 3147 is a two-component bacteriocin produced by Lactococcus lactis subspecies lactis DPC3147. In order to further characterize the biochemical nature of the bacteriocin, both peptides were isolated which together are responsible for the antimicrobial activity. The first, LtnA1, is a 3,322 Da 30-amino acid peptide and the second component, LtnA2, is a 29-amino acid peptide with a mass of 2,847 Da. Conventional amino acid analysis revealed that both peptides contain the thioether amino acid, lanthionine, as well as an excess of alanine to that predicted from the genetic sequence of the peptides. Chiral phase gas chromatography coupled with mass spectrometry of amino acid composition indicated that both LtnA1 and LtnA2 contain D-alanine residues and amino acid sequence analysis of LtnA1 confirmed that the D-alanine results from post-translational modification of a serine residue in the primary translation product. Taken together, these results demonstrate that lacticin 3147 is a novel, two-component, D-alanine containing lantibiotic that undergoes extensive post-translational modification which may account for its potent antimicrobial activity against a wide range of Gram-positive bacteria.
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Full list of authors on original publication

C Hill, R P Ross, G Jung, H G Sahl, M Josten, R W Jack, M P Ryan

Experts in our system

Colin Hill
University College Cork
Total Publications: 351
R Paul Ross
Total Publications: 441
Michael P. Ryan
University College Dublin
Total Publications: 80