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Identification of α- d -glucose-1-phosphate cytidylyltransferase involved in Ebosin biosynthesis of Streptomyces sp. 139

Ebosin, a novel exopolysaccharide produced by Streptomyces sp. 139 has antagonist activity for IL-1R in vitro and remarkable anti-rheumatic arthritis activity in vivo. Its biosynthesis gene cluster ( ste ) has been identified. In this study, gene ste17 was expressed in Escherichia coli BL21 and the... Full description

Journal Title: Applied Microbiology and Biotechnology 2009, Vol.83(2), pp.361-368
Main Author: Qi, Xiao-Qiang
Other Authors: Sun, Qing-Li , Bai, Li-Ping , Shan, Jun-Jie , Zhang, Yang , Zhang, Ren , Li, Yuan
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0175-7598 ; E-ISSN: 1432-0614 ; DOI: 10.1007/s00253-009-1950-7
Link: http://dx.doi.org/10.1007/s00253-009-1950-7
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recordid: springer_jour10.1007/s00253-009-1950-7
title: Identification of α- d -glucose-1-phosphate cytidylyltransferase involved in Ebosin biosynthesis of Streptomyces sp. 139
format: Article
creator:
  • Qi, Xiao-Qiang
  • Sun, Qing-Li
  • Bai, Li-Ping
  • Shan, Jun-Jie
  • Zhang, Yang
  • Zhang, Ren
  • Li, Yuan
subjects:
  • gene
  • CDP--glucose synthase
  • Gene disruption
  • Biosynthesis of exopolysaccharide
  • Streptomyces
ispartof: Applied Microbiology and Biotechnology, 2009, Vol.83(2), pp.361-368
description: Ebosin, a novel exopolysaccharide produced by Streptomyces sp. 139 has antagonist activity for IL-1R in vitro and remarkable anti-rheumatic arthritis activity in vivo. Its biosynthesis gene cluster ( ste ) has been identified. In this study, gene ste17 was expressed in Escherichia coli BL21 and the recombinant protein was purified. With CTP and α- d -glucose-1-phosphate as substrates, the recombinant Ste17 protein was found capable of catalyzing the production of CDP- d -glucose and pyrophosphate, demonstrating its identity as an α- d -glucose-1-phosphate–cytidylyltransferase (CDP- d -glucose synthase). To investigate the function of ste17 in Ebosin biosynthesis, the gene was disrupted with a double crossover via homologous recombination. The monosaccharide composition of exopolysaccharide (EPS) produced by the mutant Streptomyces sp. 139 ( ste17 − ) was found significantly altered from that of Ebosin, with glucose becoming undetectable. This gene knockout also negatively affected the antagonist activity for IL-1R of EPS. These results indicate that the CDP- d -glucose synthase encoded by ste17 gene is involved in the formation of nucleotide sugar (CDP- d -glucose) as glucose precursor in Ebosin biosynthesis.
language: eng
source:
identifier: ISSN: 0175-7598 ; E-ISSN: 1432-0614 ; DOI: 10.1007/s00253-009-1950-7
fulltext: fulltext
issn:
  • 1432-0614
  • 14320614
  • 0175-7598
  • 01757598
url: Link


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titleIdentification of α- d -glucose-1-phosphate cytidylyltransferase involved in Ebosin biosynthesis of Streptomyces sp. 139
creatorQi, Xiao-Qiang ; Sun, Qing-Li ; Bai, Li-Ping ; Shan, Jun-Jie ; Zhang, Yang ; Zhang, Ren ; Li, Yuan
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subjectgene ; CDP--glucose synthase ; Gene disruption ; Biosynthesis of exopolysaccharide ; Streptomyces
descriptionEbosin, a novel exopolysaccharide produced by Streptomyces sp. 139 has antagonist activity for IL-1R in vitro and remarkable anti-rheumatic arthritis activity in vivo. Its biosynthesis gene cluster ( ste ) has been identified. In this study, gene ste17 was expressed in Escherichia coli BL21 and the recombinant protein was purified. With CTP and α- d -glucose-1-phosphate as substrates, the recombinant Ste17 protein was found capable of catalyzing the production of CDP- d -glucose and pyrophosphate, demonstrating its identity as an α- d -glucose-1-phosphate–cytidylyltransferase (CDP- d -glucose synthase). To investigate the function of ste17 in Ebosin biosynthesis, the gene was disrupted with a double crossover via homologous recombination. The monosaccharide composition of exopolysaccharide (EPS) produced by the mutant Streptomyces sp. 139 ( ste17 − ) was found significantly altered from that of Ebosin, with glucose becoming undetectable. This gene knockout also negatively affected the antagonist activity for IL-1R of EPS. These results indicate that the CDP- d -glucose synthase encoded by ste17 gene is involved in the formation of nucleotide sugar (CDP- d -glucose) as glucose precursor in Ebosin biosynthesis.
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descriptionEbosin, a novel exopolysaccharide produced by Streptomyces sp. 139 has antagonist activity for IL-1R in vitro and remarkable anti-rheumatic arthritis activity in vivo. Its biosynthesis gene cluster ( ste ) has been identified. In this study, gene ste17 was expressed in Escherichia coli BL21 and the recombinant protein was purified. With CTP and α- d -glucose-1-phosphate as substrates, the recombinant Ste17 protein was found capable of catalyzing the production of CDP- d -glucose and pyrophosphate, demonstrating its identity as an α- d -glucose-1-phosphate–cytidylyltransferase (CDP- d -glucose synthase). To investigate the function of ste17 in Ebosin biosynthesis, the gene was disrupted with a double crossover via homologous recombination. The monosaccharide composition of exopolysaccharide (EPS) produced by the mutant Streptomyces sp. 139 ( ste17 − ) was found significantly altered from that of Ebosin, with glucose becoming undetectable. This gene knockout also negatively affected the antagonist activity for IL-1R of EPS. These results indicate that the CDP- d -glucose synthase encoded by ste17 gene is involved in the formation of nucleotide sugar (CDP- d -glucose) as glucose precursor in Ebosin biosynthesis.
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abstractEbosin, a novel exopolysaccharide produced by Streptomyces sp. 139 has antagonist activity for IL-1R in vitro and remarkable anti-rheumatic arthritis activity in vivo. Its biosynthesis gene cluster ( ste ) has been identified. In this study, gene ste17 was expressed in Escherichia coli BL21 and the recombinant protein was purified. With CTP and α- d -glucose-1-phosphate as substrates, the recombinant Ste17 protein was found capable of catalyzing the production of CDP- d -glucose and pyrophosphate, demonstrating its identity as an α- d -glucose-1-phosphate–cytidylyltransferase (CDP- d -glucose synthase). To investigate the function of ste17 in Ebosin biosynthesis, the gene was disrupted with a double crossover via homologous recombination. The monosaccharide composition of exopolysaccharide (EPS) produced by the mutant Streptomyces sp. 139 ( ste17 − ) was found significantly altered from that of Ebosin, with glucose becoming undetectable. This gene knockout also negatively affected the antagonist activity for IL-1R of EPS. These results indicate that the CDP- d -glucose synthase encoded by ste17 gene is involved in the formation of nucleotide sugar (CDP- d -glucose) as glucose precursor in Ebosin biosynthesis.
copBerlin/Heidelberg
pubSpringer-Verlag
doi10.1007/s00253-009-1950-7
pages361-368
date2009-05