Ring A of nukacin ISK-1: A lipid II-binding motif for type-A(II) lantibiotic

Mohammad R. Islam, Mami Nishie, Jun Ichi Nagao, Takeshi Zendo, Sandro Keller, Jiro Nakayama, Daisuke Kohda, Hans Georg Sahl, Kenji Sonomoto

研究成果: ジャーナルへの寄稿記事

41 引用 (Scopus)

抄録

Ring A of nukacin ISK-1, which is also present in different type-A(II) lantibiotics, resembles a lipid II-binding motif (TxS/TxD/EC, x denotes undefined residues) similar to that present in mersacidin (type-B lantibiotics), which suggests that nukacin ISK-1 binds to lipid II as a docking molecule. Results from our experiments on peptidoglycan precursor (UDP-MurNAc-pp) accumulation and peptide antagonism assays clearly indicated that nukacin ISK-1 inhibits cell-wall biosynthesis, accumulating lipid II precursor inside the cell, and the peptide activity can be repressed by lipid I and lipid II. Interaction analysis of nukacin ISK-1 and different ring A variants with lipid II revealed that nukacin ISK-1 and nukacin D13E (a more active variant) have a high affinity (K D = 0.17 and 0.19 μM, respectively) for lipid II, whereas nukacin D13A (a less active variant) showed a lower affinity, and nukacin C14S (a negative variant lacking the ring A structure) exhibited no interaction. Therefore, on the basis of the structural similarity and positional significance of the amino acids in this region, we concluded that nukacin ISK-1 binds lipid II via its ring A region and may lead to the inhibition of cell-wall biosynthesis.

元の言語英語
ページ(範囲)3687-3690
ページ数4
ジャーナルJournal of the American Chemical Society
134
発行部数8
DOI
出版物ステータス出版済み - 2 29 2012

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Bacteriocins
Lipids
Biosynthesis
Cell Wall
Peptides
Uridine Diphosphate
Peptidoglycan
nukacin ISK-1
muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol
Assays
Amino acids
Cells
Amino Acids
Molecules

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

これを引用

Ring A of nukacin ISK-1 : A lipid II-binding motif for type-A(II) lantibiotic. / Islam, Mohammad R.; Nishie, Mami; Nagao, Jun Ichi; Zendo, Takeshi; Keller, Sandro; Nakayama, Jiro; Kohda, Daisuke; Sahl, Hans Georg; Sonomoto, Kenji.

:: Journal of the American Chemical Society, 巻 134, 番号 8, 29.02.2012, p. 3687-3690.

研究成果: ジャーナルへの寄稿記事

Islam, Mohammad R. ; Nishie, Mami ; Nagao, Jun Ichi ; Zendo, Takeshi ; Keller, Sandro ; Nakayama, Jiro ; Kohda, Daisuke ; Sahl, Hans Georg ; Sonomoto, Kenji. / Ring A of nukacin ISK-1 : A lipid II-binding motif for type-A(II) lantibiotic. :: Journal of the American Chemical Society. 2012 ; 巻 134, 番号 8. pp. 3687-3690.
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abstract = "Ring A of nukacin ISK-1, which is also present in different type-A(II) lantibiotics, resembles a lipid II-binding motif (TxS/TxD/EC, x denotes undefined residues) similar to that present in mersacidin (type-B lantibiotics), which suggests that nukacin ISK-1 binds to lipid II as a docking molecule. Results from our experiments on peptidoglycan precursor (UDP-MurNAc-pp) accumulation and peptide antagonism assays clearly indicated that nukacin ISK-1 inhibits cell-wall biosynthesis, accumulating lipid II precursor inside the cell, and the peptide activity can be repressed by lipid I and lipid II. Interaction analysis of nukacin ISK-1 and different ring A variants with lipid II revealed that nukacin ISK-1 and nukacin D13E (a more active variant) have a high affinity (K D = 0.17 and 0.19 μM, respectively) for lipid II, whereas nukacin D13A (a less active variant) showed a lower affinity, and nukacin C14S (a negative variant lacking the ring A structure) exhibited no interaction. Therefore, on the basis of the structural similarity and positional significance of the amino acids in this region, we concluded that nukacin ISK-1 binds lipid II via its ring A region and may lead to the inhibition of cell-wall biosynthesis.",
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AU - Zendo, Takeshi

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AU - Sahl, Hans Georg

AU - Sonomoto, Kenji

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