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Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins

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Published copy (DOI)

Author(s)

  • Judith Stepper
  • Shilpa Shastri
  • Trevor S Loo
  • Joanne C Preston
  • Petr Novak
  • Petr Man
  • Christopher H Moore
  • Vladimír Havlíček
  • Mark L Patchett
  • Gillian E Norris

Department/unit(s)

Publication details

JournalFEBS Letters
DatePublished - 18 Feb 2011
Issue number4
Volume585
Number of pages6
Pages (from-to)645-50
Original languageEnglish

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.

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