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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
Author(s) -
Kuipers Oscar P.,
Rollema Harry S.,
de Vos Willem M.,
Siezen Roland J.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80911-d
Subject(s) - nisin , lantibiotics , lactococcus lactis , bacillus subtilis , bacteriocin , biochemistry , peptide , peptide sequence , biology , chemistry , gene , bacteria , microbiology and biotechnology , antimicrobial , genetics , lactic acid
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 1 H‐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.