Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins.
FEBS Lett, 2011/2/18;585(4):645-50.
Stepper J[1], Shastri S, Loo TS, Preston JC, Novak P, Man P, Moore CH, Havlíček V, Patchett ML, Norris GE
Affiliations
PMID: 21251913DOI: 10.1016/j.febslet.2011.01.023
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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.
MeSH terms
Acetylglucosamine; Bacillus subtilis; Bacteriocins; Base Sequence; Circular Dichroism; Cysteine; Glycopeptides; Glycosylation; Gram-Positive Bacteria; Hexosamines; Inhibitory Concentration 50; Lactobacillales; Lactobacillus plantarum; Mass Spectrometry; Molecular Sequence Data; Peptide Fragments; Peptides; Protein Processing, Post-Translational; Protein Sorting Signals; Serine
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