Biosynthesis of Chuangxinmycin Featuring a Deubiquitinase‐like Sulfurtransferase

The knowledge on sulfur incorporation mechanism involved in sulfur‐containing molecule biosynthesis remains limited. Chuangxinmycin is a sulfur‐containing antibiotic with a unique thiopyrano[4,3,2‐cd]indole (TPI) skeleton and selective inhibitory activity against bacterial tryptophanyl‐tRNA syntheta...

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Published inAngewandte Chemie International Edition Vol. 60; no. 46; pp. 24418 - 24423
Main Authors Zhang, Xingwang, Xu, Xiaokun, You, Cai, Yang, Chaofan, Guo, Jiawei, Sang, Moli, Geng, Ce, Cheng, Fangyuan, Du, Lei, Shen, Yuemao, Wang, Sheng, Lan, Haidong, Yang, Fan, Li, Yuezhong, Tang, Ya‐Jie, Zhang, Youming, Bian, Xiaoying, Li, Shengying, Zhang, Wei
Format Journal Article
LanguageEnglish
Published WEINHEIM Wiley 08.11.2021
Wiley Subscription Services, Inc
EditionInternational ed. in English
Subjects
Actinoplanes - genetics
Actinoplanes - metabolism
Anti-Bacterial Agents - biosynthesis
Anti-Bacterial Agents - chemistry
Antibiotics
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biosynthesis
Chemistry
Chemistry, Multidisciplinary
chuangxinmycin
C−S bond biosynthesis
deubiquitinase-like protein
Escherichia coli - chemistry
Escherichia coli - genetics
Escherichia coli - metabolism
Gene clusters
Humans
Indoles - analysis
Indoles - chemistry
Indoles - metabolism
Multigene Family
Physical Sciences
Proteins
Pyrococcus - enzymology
Pyrococcus - genetics
Science & Technology
Sulfur
Sulfur - metabolism
Sulfurtransferase
Sulfurtransferases - chemistry
Sulfurtransferases - genetics
Sulfurtransferases - metabolism
tRNA
Ubiquitin
Ubiquitination
Ubiquitins - genetics
Ubiquitins - metabolism
chuangxinmycin
ACTIVATION
POTENT
C-S bond biosynthesis
PROTEIN
sulfurtransferase
PATHWAY
CHEMISTRY
SULFUR
deubiquitinase-like protein
THIAMIN
sulfur metabolism
C−S bond biosynthesis
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Abstract The knowledge on sulfur incorporation mechanism involved in sulfur‐containing molecule biosynthesis remains limited. Chuangxinmycin is a sulfur‐containing antibiotic with a unique thiopyrano[4,3,2‐cd]indole (TPI) skeleton and selective inhibitory activity against bacterial tryptophanyl‐tRNA synthetase. Despite the previously reported biosynthetic gene clusters and the recent functional characterization of a P450 enzyme responsible for C−S bond formation, the enzymatic mechanism for sulfur incorporation remains unknown. Here, we resolve this central biosynthetic problem by in vitro biochemical characterization of the key enzymes and reconstitute the TPI skeleton in a one‐pot enzymatic reaction. We reveal that the JAMM/MPN+ protein Cxm3 functions as a deubiquitinase‐like sulfurtransferase to catalyze a non‐classical sulfur‐transfer reaction by interacting with the ubiquitin‐like sulfur carrier protein Cxm4GG. This finding adds a new mechanism for sulfurtransferase in nature. Biochemical basis of the sulfur‐incorporation reaction during chuangxinmycin biosynthesis is elucidated. Particularly, the deubiquitinase‐like Cxm3 stands for the first JAMM/MPN+ family protein catalyzing a sulfur‐transfer reaction, instead of the typical amido‐bond hydrolysis reaction, by interacting with a ubiquitin‐like sulfur carrier protein Cxm4GG.
AbstractList The knowledge on sulfur incorporation mechanism involved in sulfur‐containing molecule biosynthesis remains limited. Chuangxinmycin is a sulfur‐containing antibiotic with a unique thiopyrano[4,3,2‐cd]indole (TPI) skeleton and selective inhibitory activity against bacterial tryptophanyl‐tRNA synthetase. Despite the previously reported biosynthetic gene clusters and the recent functional characterization of a P450 enzyme responsible for C−S bond formation, the enzymatic mechanism for sulfur incorporation remains unknown. Here, we resolve this central biosynthetic problem by in vitro biochemical characterization of the key enzymes and reconstitute the TPI skeleton in a one‐pot enzymatic reaction. We reveal that the JAMM/MPN+ protein Cxm3 functions as a deubiquitinase‐like sulfurtransferase to catalyze a non‐classical sulfur‐transfer reaction by interacting with the ubiquitin‐like sulfur carrier protein Cxm4GG. This finding adds a new mechanism for sulfurtransferase in nature.
The knowledge on sulfur incorporation mechanism involved in sulfur-containing molecule biosynthesis remains limited. Chuangxinmycin is a sulfur-containing antibiotic with a unique thiopyrano[4,3,2-cd]indole (TPI) skeleton and selective inhibitory activity against bacterial tryptophanyl-tRNA synthetase. Despite the previously reported biosynthetic gene clusters and the recent functional characterization of a P450 enzyme responsible for C-S bond formation, the enzymatic mechanism for sulfur incorporation remains unknown. Here, we resolve this central biosynthetic problem by in vitro biochemical characterization of the key enzymes and reconstitute the TPI skeleton in a one-pot enzymatic reaction. We reveal that the JAMM/MPN protein Cxm3 functions as a deubiquitinase-like sulfurtransferase to catalyze a non-classical sulfur-transfer reaction by interacting with the ubiquitin-like sulfur carrier protein Cxm4GG. This finding adds a new mechanism for sulfurtransferase in nature.
The knowledge on sulfur incorporation mechanism involved in sulfur‐containing molecule biosynthesis remains limited. Chuangxinmycin is a sulfur‐containing antibiotic with a unique thiopyrano[4,3,2‐cd]indole (TPI) skeleton and selective inhibitory activity against bacterial tryptophanyl‐tRNA synthetase. Despite the previously reported biosynthetic gene clusters and the recent functional characterization of a P450 enzyme responsible for C−S bond formation, the enzymatic mechanism for sulfur incorporation remains unknown. Here, we resolve this central biosynthetic problem by in vitro biochemical characterization of the key enzymes and reconstitute the TPI skeleton in a one‐pot enzymatic reaction. We reveal that the JAMM/MPN+ protein Cxm3 functions as a deubiquitinase‐like sulfurtransferase to catalyze a non‐classical sulfur‐transfer reaction by interacting with the ubiquitin‐like sulfur carrier protein Cxm4GG. This finding adds a new mechanism for sulfurtransferase in nature. Biochemical basis of the sulfur‐incorporation reaction during chuangxinmycin biosynthesis is elucidated. Particularly, the deubiquitinase‐like Cxm3 stands for the first JAMM/MPN+ family protein catalyzing a sulfur‐transfer reaction, instead of the typical amido‐bond hydrolysis reaction, by interacting with a ubiquitin‐like sulfur carrier protein Cxm4GG.
The knowledge on sulfur incorporation mechanism involved in sulfur-containing molecule biosynthesis remains limited. Chuangxinmycin is a sulfur-containing antibiotic with a unique thiopyrano[4,3,2-cd]indole (TPI) skeleton and selective inhibitory activity against bacterial tryptophanyl-tRNA synthetase. Despite the previously reported biosynthetic gene clusters and the recent functional characterization of a P450 enzyme responsible for C-S bond formation, the enzymatic mechanism for sulfur incorporation remains unknown. Here, we resolve this central biosynthetic problem by in vitro biochemical characterization of the key enzymes and reconstitute the TPI skeleton in a one-pot enzymatic reaction. We reveal that the JAMM/MPN+ protein Cxm3 functions as a deubiquitinase-like sulfurtransferase to catalyze a non-classical sulfur-transfer reaction by interacting with the ubiquitin-like sulfur carrier protein Cxm4GG. This finding adds a new mechanism for sulfurtransferase in nature.The knowledge on sulfur incorporation mechanism involved in sulfur-containing molecule biosynthesis remains limited. Chuangxinmycin is a sulfur-containing antibiotic with a unique thiopyrano[4,3,2-cd]indole (TPI) skeleton and selective inhibitory activity against bacterial tryptophanyl-tRNA synthetase. Despite the previously reported biosynthetic gene clusters and the recent functional characterization of a P450 enzyme responsible for C-S bond formation, the enzymatic mechanism for sulfur incorporation remains unknown. Here, we resolve this central biosynthetic problem by in vitro biochemical characterization of the key enzymes and reconstitute the TPI skeleton in a one-pot enzymatic reaction. We reveal that the JAMM/MPN+ protein Cxm3 functions as a deubiquitinase-like sulfurtransferase to catalyze a non-classical sulfur-transfer reaction by interacting with the ubiquitin-like sulfur carrier protein Cxm4GG. This finding adds a new mechanism for sulfurtransferase in nature.
The knowledge on sulfur incorporation mechanism involved in sulfur‐containing molecule biosynthesis remains limited. Chuangxinmycin is a sulfur‐containing antibiotic with a unique thiopyrano[4,3,2‐ cd ]indole (TPI) skeleton and selective inhibitory activity against bacterial tryptophanyl‐tRNA synthetase. Despite the previously reported biosynthetic gene clusters and the recent functional characterization of a P450 enzyme responsible for C−S bond formation, the enzymatic mechanism for sulfur incorporation remains unknown. Here, we resolve this central biosynthetic problem by in vitro biochemical characterization of the key enzymes and reconstitute the TPI skeleton in a one‐pot enzymatic reaction. We reveal that the JAMM/MPN + protein Cxm3 functions as a deubiquitinase‐like sulfurtransferase to catalyze a non‐classical sulfur‐transfer reaction by interacting with the ubiquitin‐like sulfur carrier protein Cxm4GG. This finding adds a new mechanism for sulfurtransferase in nature.
The knowledge on sulfur incorporation mechanism involved in sulfur-containing molecule biosynthesis remains limited. Chuangxinmycin is a sulfur-containing antibiotic with a unique thiopyrano[4,3,2-cd]indole (TPI) skeleton and selective inhibitory activity against bacterial tryptophanyl-tRNA synthetase. Despite the previously reported biosynthetic gene clusters and the recent functional characterization of a P450 enzyme responsible for C-S bond formation, the enzymatic mechanism for sulfur incorporation remains unknown. Here, we resolve this central biosynthetic problem by in vitro biochemical characterization of the key enzymes and reconstitute the TPI skeleton in a one-pot enzymatic reaction. We reveal that the JAMM/MPN+ protein Cxm3 functions as a deubiquitinase-like sulfurtransferase to catalyze a non-classical sulfur-transfer reaction by interacting with the ubiquitin-like sulfur carrier protein Cxm4GG. This finding adds a new mechanism for sulfurtransferase in nature.
Author Du, Lei
Zhang, Youming
You, Cai
Zhang, Wei
Xu, Xiaokun
Sang, Moli
Cheng, Fangyuan
Bian, Xiaoying
Guo, Jiawei
Wang, Sheng
Yang, Chaofan
Geng, Ce
Yang, Fan
Tang, Ya‐Jie
Shen, Yuemao
Li, Yuezhong
Li, Shengying
Zhang, Xingwang
Lan, Haidong
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Issue 46
Keywords chuangxinmycin
ACTIVATION
POTENT
C-S bond biosynthesis
PROTEIN
sulfurtransferase
PATHWAY
CHEMISTRY
SULFUR
deubiquitinase-like protein
THIAMIN
sulfur metabolism
C−S bond biosynthesis
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Snippet The knowledge on sulfur incorporation mechanism involved in sulfur‐containing molecule biosynthesis remains limited. Chuangxinmycin is a sulfur‐containing...
The knowledge on sulfur incorporation mechanism involved in sulfur-containing molecule biosynthesis remains limited. Chuangxinmycin is a sulfur-containing...
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SubjectTerms Actinoplanes - genetics
Actinoplanes - metabolism
Anti-Bacterial Agents - biosynthesis
Anti-Bacterial Agents - chemistry
Antibiotics
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biosynthesis
Chemistry
Chemistry, Multidisciplinary
chuangxinmycin
C−S bond biosynthesis
deubiquitinase-like protein
Escherichia coli - chemistry
Escherichia coli - genetics
Escherichia coli - metabolism
Gene clusters
Humans
Indoles - analysis
Indoles - chemistry
Indoles - metabolism
Multigene Family
Physical Sciences
Proteins
Pyrococcus - enzymology
Pyrococcus - genetics
Science & Technology
Sulfur
Sulfur - metabolism
Sulfurtransferase
Sulfurtransferases - chemistry
Sulfurtransferases - genetics
Sulfurtransferases - metabolism
tRNA
Ubiquitin
Ubiquitination
Ubiquitins - genetics
Ubiquitins - metabolism
Title Biosynthesis of Chuangxinmycin Featuring a Deubiquitinase‐like Sulfurtransferase
URI https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fanie.202107745
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https://www.ncbi.nlm.nih.gov/pubmed/34498345
https://www.proquest.com/docview/2587784797
https://www.proquest.com/docview/2571053606
Volume 60
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