NisC Binds the FxLx Motif of the Nisin Leader Peptide

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• 作者：Andr茅 Abts ; Manuel Montalban-Lopez ; Oscar P. Kuipers ; Sander H. Smits ; Lutz Schmitt
• 刊名：Biochemistry
• 出版年：2013
• 出版时间：August 13, 2013
• 年：2013
• 卷：52
• 期：32
• 页码：5387-5395
• 全文大小：479K
• 年卷期：v.52,no.32(August 13, 2013)
• ISSN：1520-4995

文摘

Nisin is a model system for lantibiotics, a class of peptides displaying antimicrobial activity against various Gram-positive bacteria. After ribosomal synthesis, the precursor peptide is modified in two steps, of which the last one involves consecutive cyclization reactions mediated by the cyclase NisC. Here, we present a detailed in vitro study of the interaction between NisC and the nisin precursor peptide. Our results unravel a specific interaction of NisC with the leader peptide independent of the maturation state. Furthermore, mutagenesis studies identified a specific binding sequence within the leader. Two amino acids (F_鈥?8 and L_鈥?6) within the highly conserved -FNLD- box of class I lantibiotics are essential for binding. They represent a potential general binding motif between leader peptides of a group of lantibiotics with their cyclase family. In summary, these in vitro data provide a new perception on the complexity of the lantibiotic modification machineries.