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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Anti-Bacterial Agents*
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Bacillus subtilis / genetics
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Bacillus subtilis / metabolism*
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Bacterial Proteins*
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Bacteriocins
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Base Sequence
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Cloning, Molecular
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DNA, Bacterial
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Lactococcus lactis / metabolism*
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Magnetic Resonance Spectroscopy
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Molecular Sequence Data
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Nisin / analogs & derivatives*
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Nisin / biosynthesis
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Nisin / chemistry
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Nisin / metabolism
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Peptides*
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Peptides, Cyclic / genetics
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Peptides, Cyclic / metabolism
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Protein Precursors / biosynthesis*
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Protein Precursors / genetics
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Protein Precursors / metabolism
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Protein Sorting Signals / genetics
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Protein Sorting Signals / metabolism*
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Recombinant Fusion Proteins / biosynthesis
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Sequence Homology, Amino Acid
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Trypsin
Substances
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Anti-Bacterial Agents
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Bacterial Proteins
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Bacteriocins
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DNA, Bacterial
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Peptides
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Peptides, Cyclic
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Protein Precursors
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Protein Sorting Signals
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Recombinant Fusion Proteins
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Nisin
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Trypsin
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subtilin
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nisin Z