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J Biol Chem, Vol. 274, Issue 53, 37544-37550, December 31, 1999
From the 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.
Extensive Post-translational Modification, Including Serine
to D-Alanine Conversion, in the Two-component
Lantibiotic, Lacticin 3147*
§¶,
**,,,**,§§, and Dairy Products Research Centre, Teagasc,
Moorepark, Fermoy, Co. Cork, Ireland, the § National Food
Biotechnology Centre, University College, Cork, Ireland, the
¶¶ Department of Microbiology, University College, Cork,
Ireland, ECHAZ Microcollections, Sindelfinger-Str-3, 720700 Tübingen, Germany, the ** Institute for Organic Chemistry,
University of Tübingen 720700 Tübingen, Germany, and the
Institute for Medical Microbiology and
Immunology, University of Bonn, Sigmund-Freund-Str-25, 53105, Bonn, Germany
*
This work was supported in part by a grant-in-aid under the
Food Sub-Program of the Operational Program for Industrial Development, which is administered by the Irish Department of Agriculture, Food and
Forestry, the National and European Union funds, the Deutsche
Forschungsgemeinschaft (Sonderforschungsbereich 323).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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