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Structural Diversification of Lyngbyatoxin A by Host‐Dependent Heterologous Expression of the tleABC Biosynthetic Gene Cluster

Natural products have enormous structural diversity, yet little is known about how such diversity is achieved in nature. Here we report the structural diversification of a cyanotoxin—lyngbyatoxin A—and its biosynthetic intermediates by heterologous expression of the ‐derived biosynthetic gene cluste... Full description

Journal Title: ChemBioChem 03 August 2016, Vol.17(15), pp.1407-1411
Main Author: Zhang, Lihan
Other Authors: Hoshino, Shotaro , Awakawa, Takayoshi , Wakimoto, Toshiyuki , Abe, Ikuro
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 1439-4227 ; E-ISSN: 1439-7633 ; DOI: 10.1002/cbic.201600229
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recordid: wj10.1002/cbic.201600229
title: Structural Diversification of Lyngbyatoxin A by Host‐Dependent Heterologous Expression of the tleABC Biosynthetic Gene Cluster
format: Article
creator:
  • Zhang, Lihan
  • Hoshino, Shotaro
  • Awakawa, Takayoshi
  • Wakimoto, Toshiyuki
  • Abe, Ikuro
subjects:
  • Alkaloids
  • Biosynthesis
  • Heterologous Expression
  • Natural Products
  • Pathway Crosstalk
ispartof: ChemBioChem, 03 August 2016, Vol.17(15), pp.1407-1411
description: Natural products have enormous structural diversity, yet little is known about how such diversity is achieved in nature. Here we report the structural diversification of a cyanotoxin—lyngbyatoxin A—and its biosynthetic intermediates by heterologous expression of the ‐derived biosynthetic gene cluster in three different hosts: , , and . Notably, the isolated lyngbyatoxin derivatives, including four new natural products, were biosynthesized by crosstalk between the heterologous gene cluster and the endogenous host enzymes. The simple strategy described here has expanded the structural diversity of lyngbyatoxin A and its biosynthetic intermediates, and provides opportunities for investigation of the currently underestimated hidden biosynthetic crosstalk. : Heterologous expression of the teleocidin biosynthetic gene cluster in different hosts afforded new indole alkaloids, originating from all possible intermediates of the lyngbyatoxin biosynthetic pathway.
language: eng
source:
identifier: ISSN: 1439-4227 ; E-ISSN: 1439-7633 ; DOI: 10.1002/cbic.201600229
fulltext: fulltext
issn:
  • 1439-4227
  • 14394227
  • 1439-7633
  • 14397633
url: Link


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titleStructural Diversification of Lyngbyatoxin A by Host‐Dependent Heterologous Expression of the tleABC Biosynthetic Gene Cluster
creatorZhang, Lihan ; Hoshino, Shotaro ; Awakawa, Takayoshi ; Wakimoto, Toshiyuki ; Abe, Ikuro
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subjectAlkaloids ; Biosynthesis ; Heterologous Expression ; Natural Products ; Pathway Crosstalk
descriptionNatural products have enormous structural diversity, yet little is known about how such diversity is achieved in nature. Here we report the structural diversification of a cyanotoxin—lyngbyatoxin A—and its biosynthetic intermediates by heterologous expression of the ‐derived biosynthetic gene cluster in three different hosts: , , and . Notably, the isolated lyngbyatoxin derivatives, including four new natural products, were biosynthesized by crosstalk between the heterologous gene cluster and the endogenous host enzymes. The simple strategy described here has expanded the structural diversity of lyngbyatoxin A and its biosynthetic intermediates, and provides opportunities for investigation of the currently underestimated hidden biosynthetic crosstalk. : Heterologous expression of the teleocidin biosynthetic gene cluster in different hosts afforded new indole alkaloids, originating from all possible intermediates of the lyngbyatoxin biosynthetic pathway.
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titleStructural Diversification of Lyngbyatoxin A by Host‐Dependent Heterologous Expression of the tleABC Biosynthetic Gene Cluster
descriptionNatural products have enormous structural diversity, yet little is known about how such diversity is achieved in nature. Here we report the structural diversification of a cyanotoxin—lyngbyatoxin A—and its biosynthetic intermediates by heterologous expression of the ‐derived biosynthetic gene cluster in three different hosts: , , and . Notably, the isolated lyngbyatoxin derivatives, including four new natural products, were biosynthesized by crosstalk between the heterologous gene cluster and the endogenous host enzymes. The simple strategy described here has expanded the structural diversity of lyngbyatoxin A and its biosynthetic intermediates, and provides opportunities for investigation of the currently underestimated hidden biosynthetic crosstalk. : Heterologous expression of the teleocidin biosynthetic gene cluster in different hosts afforded new indole alkaloids, originating from all possible intermediates of the lyngbyatoxin biosynthetic pathway.
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titleStructural Diversification of Lyngbyatoxin A by Host‐Dependent Heterologous Expression of the tleABC Biosynthetic Gene Cluster
authorZhang, Lihan ; Hoshino, Shotaro ; Awakawa, Takayoshi ; Wakimoto, Toshiyuki ; Abe, Ikuro
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abstractNatural products have enormous structural diversity, yet little is known about how such diversity is achieved in nature. Here we report the structural diversification of a cyanotoxin—lyngbyatoxin A—and its biosynthetic intermediates by heterologous expression of the ‐derived biosynthetic gene cluster in three different hosts: , , and . Notably, the isolated lyngbyatoxin derivatives, including four new natural products, were biosynthesized by crosstalk between the heterologous gene cluster and the endogenous host enzymes. The simple strategy described here has expanded the structural diversity of lyngbyatoxin A and its biosynthetic intermediates, and provides opportunities for investigation of the currently underestimated hidden biosynthetic crosstalk. : Heterologous expression of the teleocidin biosynthetic gene cluster in different hosts afforded new indole alkaloids, originating from all possible intermediates of the lyngbyatoxin biosynthetic pathway.
doi10.1002/cbic.201600229
pages1407-1411
date2016-08-03