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

FEBS Letters

Rollema, Harry S.¹  de Vos, Willem M.¹  Kuipers, Oscar P.¹  Siezen, Roland J.¹ 

[1] Department of Biophysical Chemistry, NIZO, P.O. Box 20, 6710 BA Ede, The Netherlands

关键词: Nisin;    Subtilin;    Leader peptide;    Secretion;    Antimicrobial activity;    Lactococcus lactis;    Abu-S-Ala;    (2S;    3S;    6R)-3-methyllanthionine;    Ala-S-Ala;    (2S;    6R)-lanthionine;    Dha;    dehydroalanine;    Dhb;    dehydrobutyrine;    NMR;    nuclear magnetic resonance;    NOESY;    nuclear Overhauser effect spectroscopy;    PCR;    polymerase chain reaction;    ROESY;    rotating frame Overhauser effect spectroscopy;    RP-HPLC;    reversed-phase high-performance liquid chromatography;    sl;    subtilin leader;    TFA;    trifluoroacetic acid;    TOCSY;    total correlation spectroscopy;   

DOI  :  10.1016/0014-5793(93)80911-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown