LiaRS reporter assay: A simple tool to identify lipid II binding moieties in lantibiotic nukacin ISK-1.

Citation data:

Journal of bioscience and bioengineering, ISSN: 1347-4421, Vol: 123, Issue: 3, Page: 398-401

Publication Year:
2017
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PMID:
27856233
DOI:
10.1016/j.jbiosc.2016.10.002
Author(s):
Khaled M. Elsayed; Mohammad R. Islam; null Abdullah-Al-Mahin; Jun-ichi Nagao; Takeshi Zendo; Kenji Sonomoto
Publisher(s):
Elsevier BV
Tags:
Biochemistry, Genetics and Molecular Biology; Chemical Engineering; Immunology and Microbiology
article description
Binding to lipid II is an important step in the mode of action of most lantibiotics targeting the bacterial cell wall. We applied the Bacillus subtilis two-component system, LiaRS, that is known to respond to antibiotics interfering with lipid II cycle, in order to evaluate lipid II binding activity of known bacteriocins and also to identify lipid II binding moieties in lantibiotic nukacin ISK-1. Using this method, we confirmed that the methyllanthionine ring in nukacin ISK-1 is crucial for lipid II binding as previously indicated. In this study, we further identified that the three N-terminal lysine residues (K1, K2, and K3) and the glycine (G5) residue in nukacin ISK-1 are also important in lipid II binding.