Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins
Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins
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DOI：
10.1016/j.febslet.2011.01.023
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发表时间：
2011-02-18
期刊：
影响因子：
3.5
通讯作者：
Norris, Gillian E.
中科院分区：
文献类型：
--
作者：
Stepper, Judith;Shastri, Shilpa;Norris, Gillian E.
o糖基化是一种普遍存在的真核生物翻译后修饰，而早期关于s链糖肽的报道从未得到证实。原核生物也使蛋白质糖基化，但在核糖体抗菌多肽（统称细菌素）中没有证实的侧链糖基化的例子。本研究表明，植物乳杆菌KW30分泌的细菌素glycocin F被连接Ser18的n -乙酰氨基氨基β - o和连接c端Cys43的n -乙酰己糖胺s修饰。o -连接的n -乙酰氨基葡萄糖是抑菌活性所必需的，c端是完全有效（IC50 2 nM）所必需的。基因组背景分析鉴定了厚壁菌门中多种假定的糖肽细菌素。其中一种是著名的抗生素亚布兰辛，它含有一个与Cys22相连的己糖s。(C) 2011年欧洲生化学会联合会。Elsevier B.V.版权所有。
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 beta-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. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.