通过比较基因组学、敲除研究和外铁杆菌C的全合成研究铁杆菌疫苗和相关n -酰基酪氨酸的生物合成。

IF 6.2 2区 化学 Q1 CHEMISTRY, MULTIDISCIPLINARY
Maria Sauer, Myriel Staack, Sven Balluff, Christian Jogler, Nicolai Kallscheuer, Christine Beemelmanns
{"title":"通过比较基因组学、敲除研究和外铁杆菌C的全合成研究铁杆菌疫苗和相关n -酰基酪氨酸的生物合成。","authors":"Maria Sauer, Myriel Staack, Sven Balluff, Christian Jogler, Nicolai Kallscheuer, Christine Beemelmanns","doi":"10.1038/s42004-025-01654-4","DOIUrl":null,"url":null,"abstract":"<p><p>N-acyl tyrosines, a prominent class of N-acyl amino acid biomolecules, are produced by selected species in at least three bacterial phyla: Pseudomonadota, Actinomycetota and Planctomycetota. Long-chain N-acyl tyrosines with a characteristic 2,3-dehydrotyrosine core structure and additional taxon-specific chemical modifications were previously reported under the names thalassotalic acids, kyonggic acids and stieleriacines. However, the underlying pathway for their biosynthesis in the different bacterial taxa remains largely unexplored. Here, we focused on the identification of biosynthetic enzymes in the two known stieleriacine-producing planctomycetal strains of the eponymous genus Stieleria. Comparative genome analyses of stieleriacine-, thalassotalic acid- and kyonggic acid producers suggest a common pathway for N-acyl dehydrotyrosine biosynthesis based on conserved genes encoding a putative adenylyltransferase/cyclase, nitroreductase and the hallmark protein N-acyl amino acid synthase (NasY). The targeted deletion of three predicted nasY genes in Stieleria neptunia indicates that one of the three encoded enzymes predominantly produces stieleriacines. We also confirmed the absolute structure of stieleriacine C by synthesis of its epimer and structural derivatives, which serve as the basis for the future investigation of the biological function of N-acyl tyrosines.</p>","PeriodicalId":10529,"journal":{"name":"Communications Chemistry","volume":"8 1","pages":"283"},"PeriodicalIF":6.2000,"publicationDate":"2025-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12479983/pdf/","citationCount":"0","resultStr":"{\"title\":\"Investigations into the biosynthesis of stieleriacines and related N-acyl tyrosines by comparative genomics, knock-out studies and total synthesis of epi-stieleriacine C.\",\"authors\":\"Maria Sauer, Myriel Staack, Sven Balluff, Christian Jogler, Nicolai Kallscheuer, Christine Beemelmanns\",\"doi\":\"10.1038/s42004-025-01654-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>N-acyl tyrosines, a prominent class of N-acyl amino acid biomolecules, are produced by selected species in at least three bacterial phyla: Pseudomonadota, Actinomycetota and Planctomycetota. Long-chain N-acyl tyrosines with a characteristic 2,3-dehydrotyrosine core structure and additional taxon-specific chemical modifications were previously reported under the names thalassotalic acids, kyonggic acids and stieleriacines. However, the underlying pathway for their biosynthesis in the different bacterial taxa remains largely unexplored. Here, we focused on the identification of biosynthetic enzymes in the two known stieleriacine-producing planctomycetal strains of the eponymous genus Stieleria. Comparative genome analyses of stieleriacine-, thalassotalic acid- and kyonggic acid producers suggest a common pathway for N-acyl dehydrotyrosine biosynthesis based on conserved genes encoding a putative adenylyltransferase/cyclase, nitroreductase and the hallmark protein N-acyl amino acid synthase (NasY). The targeted deletion of three predicted nasY genes in Stieleria neptunia indicates that one of the three encoded enzymes predominantly produces stieleriacines. We also confirmed the absolute structure of stieleriacine C by synthesis of its epimer and structural derivatives, which serve as the basis for the future investigation of the biological function of N-acyl tyrosines.</p>\",\"PeriodicalId\":10529,\"journal\":{\"name\":\"Communications Chemistry\",\"volume\":\"8 1\",\"pages\":\"283\"},\"PeriodicalIF\":6.2000,\"publicationDate\":\"2025-09-29\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12479983/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Communications Chemistry\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://doi.org/10.1038/s42004-025-01654-4\",\"RegionNum\":2,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Communications Chemistry","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1038/s42004-025-01654-4","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0

摘要

n -酰基酪氨酸是一类重要的n -酰基氨基酸生物分子,由至少三个细菌门的特定物种产生:假单胞菌门、放线菌门和植菌门。长链n-酰基酪氨酸具有典型的2,3-脱氢酪氨酸核心结构和额外的分类群特异性化学修饰,以前被称为thalassotalic acid, kyonggic acids和stieleriacines。然而,它们在不同细菌分类群中生物合成的潜在途径在很大程度上仍未被探索。在这里,我们重点研究了两种已知的产铁杆菌属植物的生物合成酶的鉴定。对铁柳碱、海草酸和龙心酸的基因组比较分析表明,n -酰基脱氢酪氨酸生物合成的共同途径是基于编码腺苷基转移酶/环化酶、硝基还原酶和标志蛋白n -酰基氨基酸合成酶(nassy)的保守基因。鼠铁杆菌中三个预测的nassy基因的靶向缺失表明,三种编码酶中的一种主要产生铁铁菌素。我们还通过合成其外显体和结构衍生物确定了铁铁菌C的绝对结构,为进一步研究n -酰基酪氨酸的生物学功能奠定了基础。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Investigations into the biosynthesis of stieleriacines and related N-acyl tyrosines by comparative genomics, knock-out studies and total synthesis of epi-stieleriacine C.

N-acyl tyrosines, a prominent class of N-acyl amino acid biomolecules, are produced by selected species in at least three bacterial phyla: Pseudomonadota, Actinomycetota and Planctomycetota. Long-chain N-acyl tyrosines with a characteristic 2,3-dehydrotyrosine core structure and additional taxon-specific chemical modifications were previously reported under the names thalassotalic acids, kyonggic acids and stieleriacines. However, the underlying pathway for their biosynthesis in the different bacterial taxa remains largely unexplored. Here, we focused on the identification of biosynthetic enzymes in the two known stieleriacine-producing planctomycetal strains of the eponymous genus Stieleria. Comparative genome analyses of stieleriacine-, thalassotalic acid- and kyonggic acid producers suggest a common pathway for N-acyl dehydrotyrosine biosynthesis based on conserved genes encoding a putative adenylyltransferase/cyclase, nitroreductase and the hallmark protein N-acyl amino acid synthase (NasY). The targeted deletion of three predicted nasY genes in Stieleria neptunia indicates that one of the three encoded enzymes predominantly produces stieleriacines. We also confirmed the absolute structure of stieleriacine C by synthesis of its epimer and structural derivatives, which serve as the basis for the future investigation of the biological function of N-acyl tyrosines.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Communications Chemistry
Communications Chemistry Chemistry-General Chemistry
CiteScore
7.70
自引率
1.70%
发文量
146
审稿时长
13 weeks
期刊介绍: Communications Chemistry is an open access journal from Nature Research publishing high-quality research, reviews and commentary in all areas of the chemical sciences. Research papers published by the journal represent significant advances bringing new chemical insight to a specialized area of research. We also aim to provide a community forum for issues of importance to all chemists, regardless of sub-discipline.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信