Biosynthesis and secretion of a precursor of nisin Z by Lactococcus lactis, directed by the leader peptide of the homologous lantibiotic subtilin from Bacillus subtilis

Oscar P. Kuipers, Harry S. Rollema, Willem M. de Vos, Roland J. Siezen

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Abstract

The DNA sequence encoding the leader peptide of the lantibiotic subtilin from Bacillus subtilis was fused to the sequence encoding pronisin Z, and this hybrid gene was expressed in a Lactococcus lactis strain that produces nisin A. This strain simultaneously secreted nisin A and a protein of approximately 6 kDa Amino acid sequencing of the purified 6 kDa protein and structural analysis of its main tryptic fragment by two-dimensional 1H-NMR showed that it consists of the unmodified leader peptide of subtilin, without the N-terminal methionine residue, linked to a fully matured nisin Z part. The hybrid protein and its main tryptic fragment [ITPQ]-nisin Z, showed at least 200-fold lower antimicrobial activities than nisin Z against three different indicator strains.
Original languageEnglish
Number of pages5
JournalFEBS Letters
Volume330
Issue number1
DOIs
Publication statusPublished - 1993

Keywords

  • Lactococcus lactis
  • Antimicrobial activity
  • Secretion
  • Leader peptide
  • Subtilin
  • Nisin

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