Open AccessThe C‐terminus of nisin is important for the ABC transporter Nis FEG to confer immunity in Lactococcus lactis
Author(s) -
AlKhatib Zainab,
Lagedroste Marcel,
Zaschke Julia,
Wagner Manuel,
Abts André,
Fey Iris,
Kleinschrodt Diana,
Smits Sander H. J.
Publication year - 2014
Publication title -
microbiologyopen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.881
H-Index - 36
ISSN - 2045-8827
DOI - 10.1002/mbo3.205
Subject(s) - nisin , lantibiotics , lactococcus lactis , lipid ii , lanthionine , atp binding cassette transporter , bacteriocin , biochemistry , bacteria , lactococcus , microbiology and biotechnology , biology , chemistry , peptide , transporter , antimicrobial , enzyme , biosynthesis , lactic acid , gene , genetics
The lantibiotic nisin is a small 3.4 kD a antimicrobial peptide, which acts against Gram‐positive bacteria in the nmol/L range. Nisin is produced and secreted by several Lactococcus lactis strains to ensure advantages against other bacteria in their habitat. Nisin contains five specific lanthionine rings of which the first two are important for Lipid II binding and the last two are crucial for the pore formation in the membrane. To gain immunity against nisin, the producing strain is expressing an ABC transporter called NisFEG, which expels nisin from the membrane. As a result six to eightfold more nisin is needed to affect the cells. The hydrolysis of ATP by NisFEG is required for this immunity as shown by a mutant, where the ATP hydrolysis is disrupted (NisF H181A EG). Furthermore, NisFEG recognizes the C‐terminus of nisin, since deletion of the last six amino acids as well as of the last ring lowered the fold of immunity displayed by NisFEG.