Characterization of functional domains of lantibiotic-binding immunity protein, NukH, from Staphylococcus warneri ISK-1

Ken Ichi Okuda, Yuji Aso, Jun Ichi Nagao, Kouki Shioya, Youhei Kanemasa, Jiro Nakayama, Kenji Sonomoto

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

Abstract

The immunity to a lantibiotic, nukacin ISK-1, is conferred by NukFEG (ABC transporter) and NukH (lantibiotic-binding protein) cooperatively. The present study identifies the functional domains of NukH. The topological analysis indicated that NukH possesses two external loops and three transmembrane helices. Deletion of N or C terminus of NukH did not affect the function. Amino acids substitutions in the respective loops abolished the function. Deletion of the third transmembrane helix resulted in loss of immunity but did not affect the binding activity. These findings suggested that the whole structure of NukH, except for N and C termini, is essential for its full immunity function, and that NukH inactivates nukacin ISK-1 after binding.

Original languageEnglish
Pages (from-to)19-25
Number of pages7
JournalFEMS microbiology letters
Volume250
Issue number1
DOIs
Publication statusPublished - Sep 1 2005

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology
  • Genetics

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