Work

Discovery, Biosynthesis, and Characterization of Rodencin, a Two-Component Lanthipeptide, Harboring d -Amino Acids Introduced by the Unusual Dehydrogenase RodJA

Year: 2024

Type: article

Abstract: High Resolution Image Download MS PowerPoint Slide Lanthipeptides, a group of ribosomally synthesized and post-translationally modified peptides (RiPPs), exhibit diverse structures and bioactivities. Their biosynthetic enzymes serve as valuable tools for peptide bioengineering. Here, we report a class II lanthipeptide biosynthetic gene cluster in a Bacillus strain, driving the biosynthesis of a two-component lanthipeptide, termed rodencin, featured by the presence of two different d -amino acids, i.e., d -Ala and d -Abu. Rodencin displays synergistic antimicrobial activity against food-borne pathogens such as Bacillus cereus, Staphylococcus aureus, and Listeria monocytogenes . The α-peptide of rodencin contains one d -Ala and the β-peptide features both d -Ala and d -Abu. These are installed by dehydratases RodM1 and RodM2 and dehydrogenase RodJ A, the activities of which were successfully reconstituted using a dedicated E. coli expression system. To illustrate the unusual d -Abu incorporation potential of the enzymes, analogous to the d -amino acid-containing β peptide of lacticin 3147, was successfully produced with the rodencin heterologous expression system, by employing RodM2 and the dehydrogenase RodJ A .

Source: Journal of Natural Products

DOI: 10.1021/acs.jnatprod.4c00170

Authors: Yuxin Fu, Eleftheria Pateri, Oscar P. Kuipers

Institution: University of Groningen

Language: English

Topic: Microbial Natural Products and Biosynthesis

Subfield: Pharmacology

Field: Medicine

Domain: Health Sciences

Open Access status: hybrid

Estimated APC paid: $4,500

Funder: China Scholarship Council