TY - JOUR
T1 - Characterization of functional domains of lantibiotic-binding immunity protein, NukH, from Staphylococcus warneri ISK-1
AU - Okuda, Ken Ichi
AU - Aso, Yuji
AU - Nagao, Jun Ichi
AU - Shioya, Kouki
AU - Kanemasa, Youhei
AU - Nakayama, Jiro
AU - Sonomoto, Kenji
N1 - Funding Information:
This work was partially supported by Grants-in-Aid for Scientific Research from the Japan Society for the Promotion of Science (JSPS), by a Sasakawa Scientific Research Grant from the Japan Science Society, by JSPS research fellowships, and by the grants from the Novartis Foundation (Japan) for the Promotion of Science, the Novozymes Japan Research Fund, the Nagase Science and Technology Foundation.
PY - 2005/9/1
Y1 - 2005/9/1
N2 - 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.
AB - 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.
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U2 - 10.1016/j.femsle.2005.06.039
DO - 10.1016/j.femsle.2005.06.039
M3 - Article
C2 - 16009508
AN - SCOPUS:23744455185
VL - 250
SP - 19
EP - 25
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
SN - 0378-1097
IS - 1
ER -