Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin
Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin
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DOI：
10.1073/pnas.0900008106
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发表时间：
2009-02-24
影响因子：
11.1
通讯作者：
Fischbach, Michael A.
中科院分区：
文献类型：
--
作者：
Brown, Laura C. Wieland;Acker, Michael G.;Fischbach, Michael A.
噻唑基多肽是一类>；50杀菌抗生素，可阻断细菌蛋白质合成的初始步骤。在这里，我们报告了硫氧西林的生物合成基因簇，并确定它以及整个类别都是核糖体合成的。值得注意的是，一个52个残基的多肽前体的C-末端14个残基经历了13次翻译后修饰产生硫代西林，使这种抗生素成为迄今已知的翻译后修饰最严重的多肽。
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.