Abstract
O-Glycosylation is a ubiquitous eukaryotic post-translational modification, whereas early reports of S-linked glycopeptides have never been verified. Prokaryotes also glycosylate proteins, but there are no confirmed examples of sidechain glycosylation in ribosomal antimicrobial polypeptides collectively known as bacteriocins. Here we show that glycocin F, a bacteriocin secreted by Lactobacillus plantarum KW30, is modified by an N-acetylglucosamine β-O-linked to Ser18, and an N-acetylhexosamine S-linked to C-terminal Cys43. The O-linked N-acetylglucosamine is essential for bacteriostatic activity, and the C-terminus is required for full potency (IC(50) 2 nM). Genomic context analysis identified diverse putative glycopeptide bacteriocins in Firmicutes. One of these, the reputed lantibiotic sublancin, was shown to contain a hexose S-linked to Cys22.
Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
- Research Support, Non-U.S. Gov't
MeSH terms
- Acetylglucosamine / metabolism
- Bacillus subtilis / metabolism
- Bacteriocins / chemistry*
- Bacteriocins / genetics
- Bacteriocins / isolation & purification
- Bacteriocins / metabolism*
- Base Sequence
- Circular Dichroism
- Cysteine / metabolism*
- Glycopeptides / metabolism*
- Glycosylation
- Gram-Positive Bacteria / genetics
- Gram-Positive Bacteria / metabolism
- Hexosamines / metabolism
- Inhibitory Concentration 50
- Lactobacillales / drug effects
- Lactobacillus plantarum / metabolism
- Mass Spectrometry
- Molecular Sequence Data
- Peptide Fragments / chemistry
- Peptide Fragments / metabolism
- Peptide Fragments / pharmacology
- Peptides / chemistry
- Peptides / metabolism
- Protein Processing, Post-Translational*
- Protein Sorting Signals
- Serine
Substances
- Bacteriocins
- Glycopeptides
- Hexosamines
- Peptide Fragments
- Peptides
- Protein Sorting Signals
- glycocin F, Lactobacillus plantarum
- sublancin 168
- Serine
- Cysteine
- Acetylglucosamine