RRC ID 50674
Author Elsayed KM, Islam MR, Abdullah-Al-Mahin, Nagao JI, Zendo T, Sonomoto K.
Title LiaRS reporter assay: A simple tool to identify lipid II binding moieties in lantibiotic nukacin ISK-1.
Journal J Biosci Bioeng
Abstract 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.
Volume 123(3)
Pages 398-401
Published 2017-3-1
DOI 10.1016/j.jbiosc.2016.10.002
PII S1389-1723(16)30353-X
PMID 27856233
MeSH Alanine / analogs & derivatives Alanine / metabolism Amino Acid Sequence Bacillus subtilis / metabolism* Bacteriocins / chemistry* Bacteriocins / metabolism* Cell Wall / metabolism Genes, Reporter* Sulfides / metabolism Uridine Diphosphate N-Acetylmuramic Acid / analogs & derivatives* Uridine Diphosphate N-Acetylmuramic Acid / metabolism
IF 2.366
Times Cited 4
Resource
General Microbes JCM 1157