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Nosiheptide Biosynthesis Featuring a Unique Indole Side Ring Formation on the Characteristic Thiopeptide Framework
其他题名Nosiheptide Biosynthesis Featuring a Unique Indole Side Ring Formation on the Characteristic Thiopeptide Framework
Yu Y(虞沂); DUAN LIAN; Zhang Q(张琪); LIAO RIJING; DING YING; PAN HAIXUE; WENDTPIENKOWSKI EVELYN; Tang GL(唐功利); SHEN BEN; Liu W(刘文)
2009
发表期刊ACS Chem. Biol.
ISSN1554-8929
卷号4期号:10页码:855-864
摘要Nosiheptide (NOS), belonging to thee series of thiopeptide antibiotics that exhibit potent activity against various bacterial pathogens, bears a unique indole side ring system and regiospecific hydroxyl groups on the characteristic macrocyclic core. Here, cloning, sequencing, and characterization of the nos gene cluster from Streptomyces actuosus ATCC 25421 as a model for this series of thiopeptides has unveiled new insights Into their biosynthesis. Bioinformatics-based sequence analysis and In vivo Investigation Into the gene functions show that NOS biosynthesis shares a common strategy with recently characterized b or c series thiopeptides for forming the characteristic macrocyclic core, which features a ribosomally synthesized precursor peptide with conserved posttranslational modifications. However, it apparently proceeds via a different route for tailoring the thiopeptide framework, allowing the final product to exhibit the distinct structural characteristics of e series thiopeptides, such as the indole side ring system. Chemical complementation supports the notion that the S-adenosylmethionine-dependent protein NosL may play a central role in converting tryptophan to the key 3-methylindole moiety by an unusual carbon side chain rearrangement, most likely via a radical-initiated mechanism. Characterization of the indole side ring-opened analogue of NOS from the nosN mutant strain Is consistent with the proposed methyltransferase activity of Its encoded protein, shedding light into the timing of the individual steps for Indole side ring biosynthesis. These results also suggest the feasibility of engineering novel thiopeptides for drug discovery by manipulating the NOS biosynthetic machinery.
学科领域生命有机化学
部门归属上海有机所; 上海交通大学; 美国威斯康星大学
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收录类别SCI
语种英语
WOS记录号WOS:000272562000006
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被引频次:106[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.sioc.ac.cn/handle/331003/28455
专题生命有机化学国家重点实验室
通讯作者Liu W(刘文)
推荐引用方式
GB/T 7714
Yu Y,DUAN LIAN,Zhang Q,et al. Nosiheptide Biosynthesis Featuring a Unique Indole Side Ring Formation on the Characteristic Thiopeptide Framework[J]. ACS Chem. Biol.,2009,4(10):855-864.
APA 虞沂.,DUAN LIAN.,张琪.,LIAO RIJING.,DING YING.,...&刘文.(2009).Nosiheptide Biosynthesis Featuring a Unique Indole Side Ring Formation on the Characteristic Thiopeptide Framework.ACS Chem. Biol.,4(10),855-864.
MLA 虞沂,et al."Nosiheptide Biosynthesis Featuring a Unique Indole Side Ring Formation on the Characteristic Thiopeptide Framework".ACS Chem. Biol. 4.10(2009):855-864.
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