Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin
Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin
复制标题
DOI：
10.1073/pnas.0900008105
复制
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.
噻唑基肽是一个超过50种杀菌抗生素家族，可阻断细菌蛋白质合成的初始步骤。在这里，我们报告了一个生物合成的基因簇硫西林，并建立它，并通过扩展整个类，是核糖体合成。值得注意的是，52个残基的肽前体的C-末端14个残基经历13个翻译后修饰以产生硫代西林，使该抗生素成为迄今为止已知的最严重的翻译后修饰的肽。
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.