首页 | 本学科首页   官方微博 | 高级检索  
   检索      


Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins
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
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
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.
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
本文献已被 ScienceDirect PubMed 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号