NisC Binds the FxLx Motif of the Nisin Leader Peptide
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Abstract
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 <i>in vitro</i> 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<sub>–18</sub> and L<sub>–16</sub>) 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 <i>in vitro</i> data provide
a new perception on the complexity of the lantibiotic modification
machineries