PMID: 2493449Mar 1, 1989Paper

Nisin, a peptide antibiotic: cloning and sequencing of the nisA gene and posttranslational processing of its peptide product

Journal of Bacteriology
C Kaletta, K D Entian

Abstract

Nisin produced by Streptococcus lactis is used as a food preservative and is the most important member of a group of antibiotics containing lanthionine bridges. To understand the genetic basis of these so-called lantibiotics (Schnell et al., Nature 333:276-278, 1988), we characterized the nisin structural gene, nisA, which is located on a plasmid and codes for a 57-amino-acid prepeptide. The prepeptide is processed posttranslationally to the pentacyclic antibiotic. Although nisin and the recently elucidated lantibiotic epidermin from Staphylococcus epidermidis are produced by different organisms, their gene organization is identical. As with epidermin, the nisin propeptide corresponds to the C-terminus of the prepeptide. The N-terminus of the prepeptide is cleaved at a characteristic splice site (Pro--2 Arg--1 Ile-+1). Remarkably, the N-terminus of prenisin shares 70% similarity with preepidermin, although the propeptide sequences are distinctly different. The structural similarities between these two lantibiotics are consistent with the fact that there is a common mechanism of biosynthesis of these lanthionine-containing antibiotics.

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Citations

Feb 15, 1992·European Journal of Biochemistry·N SchnellK D Entian
Sep 1, 1990·FEMS Microbiology Reviews·L L McKay, K A Baldwin
Jan 1, 1989·Archives of Microbiology·C KalettaH G Sahl
Jun 15, 1995·European Journal of Biochemistry·H G SahlG Bierbaum
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Mar 8, 2003·Molecular Microbiology·Torsten SteinKarl-Dieter Entian
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Jul 16, 2017·Applied and Environmental Microbiology·Christoph GeigerKarl-Dieter Entian
Apr 7, 2019·Applied and Environmental Microbiology·Christoph GeigerKarl-Dieter Entian
Jul 28, 2020·Applied and Environmental Microbiology·Jiaheng LiuJianjun Qiao
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