Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins |
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Authors: | Stepper Judith Shastri Shilpa Loo Trevor S Preston Joanne C Novak Petr Man Petr Moore Christopher H Havlíček Vladimír Patchett Mark L Norris Gillian E |
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Institution: | aInstitute of Molecular Biosciences, Massey University, Palmerston North 4442, New Zealand;bInstitute of Microbiology, v.v.i., Academy of Sciences of the Czech Republic, Videnska 1083, 142 20 Prague 4, Czech Republic |
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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 (IC50 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. |
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Keywords: | Abbreviations: GccF glycocin F deOGlcNAcGccF O-deglycosylated GccF GccF1&ndash 41 peptide fragment 1&ndash 41 of GccF GlcNAc N-acetylglucosamine HexNAc N-acetylhexosamine CD circular dichroism FT-ICR-MS Fourier transform ion cyclotron resonance mass spectrometry IC50 concentration that decreases growth rate by 50% ECD electron capture dissociation TFA trifluoroacetic acid |
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