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

Khaled M. Elsayed; Mohammad R. Islam; Abdullah-Al-Mahin; Jun ichi Nagao; Takeshi Zendo; Kenji Sonomoto

doi:10.1016/j.jbiosc.2016.10.002

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

Khaled M. Elsayed, Mohammad R. Islam, Abdullah-Al-Mahin, Jun ichi Nagao, Takeshi Zendo, Kenji Sonomoto

Systems Biology

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

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.

Original language	English
Pages (from-to)	398-401
Number of pages	4
Journal	Journal of Bioscience and Bioengineering
Volume	123
Issue number	3
DOIs	https://doi.org/10.1016/j.jbiosc.2016.10.002
Publication status	Published - Mar 1 2017

All Science Journal Classification (ASJC) codes

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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title = "LiaRS reporter assay: A simple tool to identify lipid II binding moieties in lantibiotic nukacin ISK-1",

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.",

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T2 - A simple tool to identify lipid II binding moieties in lantibiotic nukacin ISK-1

AU - Elsayed, Khaled M.

AU - Islam, Mohammad R.

AU - Abdullah-Al-Mahin,

AU - Nagao, Jun ichi

AU - Zendo, Takeshi

AU - Sonomoto, Kenji

PY - 2017/3/1

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AB - 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.

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

Abstract

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