Lantibiotic biosynthesis: interactions between prelacticin 481 and its putative modification enzyme, LctM
Related Experiment Video
Updated: Oct 13, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
P Uguen1, J P Le Pennec, A Dufour
1Laboratoire de Biologie et Chimie Moléculaires, Université de Bretagne Sud, Vannes, France.
Abstract:
Class AII and AIII lantibiotics and mersacidin are antibacterial peptides containing unusual residues obtained by posttranslational modifications of prepeptides, presumably catalyzed by LanM. LctM, the LanM for lacticin 481, is essential for the production of this class AII lantibiotic. Using the yeast two-hybrid system, we showed direct contact between the prelacticin 481 and LctM, supporting the proposed LctM function. Sixteen domains are conserved between the 10 known LanM proteins, whereas three additional domains were found only in class AII LanM proteins and in MrsM, the LanM for mersacidin. All the truncated LctM proteins that we tested presented impaired LctA-binding activity.
Related Concept Videos
Inhibitors of Bacterial Protein Synthesis
Inhibitors of Gram-positive Cell Wall Synthesis
Production of Antibiotics
Clinical Significance of Antibiotic Resistance
Types of RNA
Three main types of RNA are involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). These RNAs perform diverse functions and can be broadly classified as protein-coding or non-coding RNA. Non-coding RNAs play important roles in the regulation of gene expression in response to developmental and environmental changes. Non-coding RNAs in prokaryotes can be manipulated to develop more effective antibacterial drugs for human or animal use.
RNA...
Antibiotic Selection
