1. Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins.
- Author
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Stepper J, Shastri S, Loo TS, Preston JC, Novak P, Man P, Moore CH, Havlíček V, Patchett ML, and Norris GE
- Subjects
- Acetylglucosamine metabolism, Bacillus subtilis metabolism, Bacteriocins genetics, Bacteriocins isolation & purification, Base Sequence, Circular Dichroism, 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 Sorting Signals, Serine, Bacteriocins chemistry, Bacteriocins metabolism, Cysteine metabolism, Glycopeptides metabolism, Protein Processing, Post-Translational
- 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.) more...
- Published
- 2011
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