Lantibiotic Reductase LtnJ Substrate Selectivity Assessed with a Collection of Nisin Derivatives as Substrates

Applied and Environmental Microbiology
Dongdong MuOscar P Kuipers

Abstract

Lantibiotics are potent antimicrobial peptides characterized by the presence of dehydrated amino acids, dehydroalanine and dehydrobutyrine, and (methyl)lanthionine rings. In addition to these posttranslational modifications, some lantibiotics exhibit additional modifications that usually confer increased biological activity or stability on the peptide. LtnJ is a reductase responsible for the introduction of D-alanine in the lantibiotic lacticin 3147. The conversion of L-serine into D-alanine requires dehydroalanine as the substrate, which is produced in vivo by the dehydration of serine by a lantibiotic dehydratase, i.e., LanB or LanM. In this work, we probe the substrate specificity of LtnJ using a system that combines the nisin modification machinery (dehydratase, cyclase, and transporter) and the stereospecific reductase LtnJ in Lactococcus lactis. We also describe an improvement in the production yield of this system by inserting a putative attenuator from the nisin biosynthesis gene cluster in front of the ltnJ gene. In order to clarify the sequence selectivity of LtnJ, peptides composed of truncated nisin and different mutated C-terminal tails were designed and coexpressed with LtnJ and the nisin biosynthetic machinery. I...Continue Reading

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Citations

Sep 12, 2015·Journal of the American Chemical Society·Xiao Yang, Wilfred A van der Donk
Sep 4, 2016·FEMS Microbiology Reviews·Manuel Montalbán-LópezOscar P Kuipers
Jan 31, 2017·Chemical Reviews·Lindsay M RepkaWilfred A van der Donk
Feb 27, 2018·Frontiers in Microbiology·Manuel Montalbán-LópezOscar P Kuipers
Jan 14, 2021·Biochemical Society Transactions·Fleur Ruijne, Oscar P Kuipers

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