Open AccessIdentification of distinct nisin leader peptide regions that determine interactions with the modification enzymes NisB and NisC
Author(s) -
Khusainov Rustem,
Moll Gert N.,
Kuipers Oscar P.
Publication year - 2013
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1016/j.fob.2013.05.001
Subject(s) - nisin , identification (biology) , peptide , enzyme , biology , chemistry , computational biology , biochemistry , microbiology and biotechnology , antimicrobial , botany
Nisin is the most prominent and applied bacteriocin that serves as a model for class I lantibiotics. The nisin leader peptide importantly determines interactions between precursor nisin and its modification enzymes NisB and NisC that mature nisin posttranslationally. NisB dehydrates serines and threonines, while NisC catalyzes the subsequent coupling of the formed dehydroamino acids to form lanthionines. Currently, little is known about how the nisin leader interacts with NisB and even less is known about its interactions with NisC. To investigate the nisin leader peptide requirements for functional interaction with the modification enzymes NisB and NisC, we systematically replaced six regions, of 2–4 amino acids each, with all‐alanine regions. By performing NisB and NisC co‐purification studies with these mutant leader peptides, we demonstrate that the nisin leader regions STKD(‐22‐19), FNLD(‐18‐15) and PR(‐2‐1) importantly contribute to the interactions of precursor nisin with both NisB and NisC, whereas the nisin leader region LVSV(‐14‐11) additionally contributes to the interaction of precursor nisin with NisC.