Difference between revisions of "Team:NUDT CHINA"
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<h4>You can know about us: </h4> | <h4>You can know about us: </h4> | ||
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− | + | <li> <a href="https://2015.igem.org/Team:NUDT_CHINA/Description">Project Description</a> </li> | |
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− | <p> | + | <p>For years, prokaryotic cells have been widely applied in synthetic biology and bio-engineering as the host organism. However, lacking of the compartmentation of the heterologous metabolic pathways, which results in a relevantly low concentration of substrate and enzyme, may cause a low production or efficacy of the product, especially when producing through a complex multi-enzymatic cascade. In the current study, we developed a new method to accelerate a multi-enzymatic reaction by integration of a TALE-based scaffold system into the bacteria chassis. In this system, we designed two different random DNA sequences as binding motifs, and then incorporated them into the plasmid. Meanwhile, the different TALE proteins, which could specifically target the corresponding binding motifs, were generated by the assembly of repeat-variable di-residue (RVD) part coding sequences. Subsequently, multi-enzymes were fused with these TALE proteins, which could efficiently guide the enzymes around the DNA scaffolds, enrich the local enzyme concentration, and promote the rate of reaction. The effect of the TALE-based scaffold system were tested by the fragmented GFP study and validated by the heterologous production of plant IAA through incorporating the TALE-fused IAAM and IAAH enzymes in E.coli. To the best of our knowledge, this technique might provide a powerful way in synthesizing multi-enzymatic reaction programs in prokaryotic chassis for a wide range of application.</p> |
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− | + | <li> <a href="https://2015.igem.org/Team:NUDT_CHINA/Description">Coming Soon~</a> </li> | |
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Revision as of 13:19, 14 July 2015
Welcome to iGEM 2015!
Nice to meet you! We are Team_NUDT_CHINA.
You can know about us:
Project Description
For years, prokaryotic cells have been widely applied in synthetic biology and bio-engineering as the host organism. However, lacking of the compartmentation of the heterologous metabolic pathways, which results in a relevantly low concentration of substrate and enzyme, may cause a low production or efficacy of the product, especially when producing through a complex multi-enzymatic cascade. In the current study, we developed a new method to accelerate a multi-enzymatic reaction by integration of a TALE-based scaffold system into the bacteria chassis. In this system, we designed two different random DNA sequences as binding motifs, and then incorporated them into the plasmid. Meanwhile, the different TALE proteins, which could specifically target the corresponding binding motifs, were generated by the assembly of repeat-variable di-residue (RVD) part coding sequences. Subsequently, multi-enzymes were fused with these TALE proteins, which could efficiently guide the enzymes around the DNA scaffolds, enrich the local enzyme concentration, and promote the rate of reaction. The effect of the TALE-based scaffold system were tested by the fragmented GFP study and validated by the heterologous production of plant IAA through incorporating the TALE-fused IAAM and IAAH enzymes in E.coli. To the best of our knowledge, this technique might provide a powerful way in synthesizing multi-enzymatic reaction programs in prokaryotic chassis for a wide range of application.