TY - JOUR
T1 - Localization and interaction of the biosynthetic proteins for the lantibiotic, nukacin ISK-1
AU - Nagao, Jun Ichi
AU - Aso, Yuji
AU - Sashihara, Toshihiro
AU - Shioya, Kouki
AU - Adachi, Asaho
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, and the Nagase Science and Technology Foundation.
PY - 2005
Y1 - 2005
N2 - Nukacin ISK-1 is a type-A(II) lantibiotic produced by Staphylococcus warneri ISK-1. In this study, we characterized NukM and NukT, which are predicted to be involved in modification of prepeptide (NukA) and cleavage of leader peptide and subsequent secretion respectively. Localization analysis of NukM and NukT in the wild-type strain indicated that both proteins were located at the cytoplasm membrane. Interestingly, NukM expressed heterologously in St. carnosus TM300 was also located at the cytoplasm membrane even in the absence of NukT. Yeast two-hybrid assay showed that a complex of at least two each of NukM and NukT was associated with NukA. In vitro interaction analysis by surface plasmon resonance biosensor further suggested that membrane-located NukM interacted with NukA. These results indicate that NukM and NukT form a membrane-located multimeric protein complex and that post-translational modification of nukacin ISK-1 would occur at the cytoplasm membrane.
AB - Nukacin ISK-1 is a type-A(II) lantibiotic produced by Staphylococcus warneri ISK-1. In this study, we characterized NukM and NukT, which are predicted to be involved in modification of prepeptide (NukA) and cleavage of leader peptide and subsequent secretion respectively. Localization analysis of NukM and NukT in the wild-type strain indicated that both proteins were located at the cytoplasm membrane. Interestingly, NukM expressed heterologously in St. carnosus TM300 was also located at the cytoplasm membrane even in the absence of NukT. Yeast two-hybrid assay showed that a complex of at least two each of NukM and NukT was associated with NukA. In vitro interaction analysis by surface plasmon resonance biosensor further suggested that membrane-located NukM interacted with NukA. These results indicate that NukM and NukT form a membrane-located multimeric protein complex and that post-translational modification of nukacin ISK-1 would occur at the cytoplasm membrane.
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U2 - 10.1271/bbb.69.1341
DO - 10.1271/bbb.69.1341
M3 - Article
C2 - 16041140
AN - SCOPUS:23944499889
VL - 69
SP - 1341
EP - 1347
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 7
ER -