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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin
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Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin

机译:十三种翻译后修饰将14个残基的肽转化为抗生素thiocillin

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摘要

The thiazolylpeptides are a family of >50 bactericidal antibiotics that block the initial steps of bacterial protein synthesis. Here, we report a biosynthetic gene cluster for thiocillin and establish that it, and by extension the whole class, is ribosomally synthesized. Remarkably, the C-terminal 14 residues of a 52-residue peptide precursor undergo 13 posttranslational modifications to give rise to thiocillin, making this antibiotic the most heavily posttranslationally-modified peptide known to date.
机译:噻唑肽是一类> 50种杀菌抗生素,可阻止细菌蛋白质合成的初始步骤。在这里,我们报告了硫代西林的生物合成基因簇,并确定它和通过扩展整个类是核糖体合成的。值得注意的是,一个52个残基的肽前体的C末端14个残基经过13个翻译后修饰,生成thiocillin,使该抗生素成为迄今为止已知的最重的翻译后修饰肽。

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