Team:Missouri Miners

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<img src="https://static.igem.org/mediawiki/2012/1/18/Missouri_Miners_Banner.png" alt="Missouri Miners 2012"/>
<img src="https://static.igem.org/mediawiki/2012/1/18/Missouri_Miners_Banner.png" alt="Missouri Miners 2012"/>
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<h1>Abstract</h1>
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<h1>Adjustable Multi-Enzyme to Cell Surface Anchoring Protein</h1>
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<p>There are a plethora of enzymes that occur in the natural world which perform reactions that could be immensely useful to humans. Unfortunately the efficiency of some of these reactions may render their applications logistically unrealistic. The cellulosome scaffolding protein produced by Clostridium thermocellum has been shown to significantly increase the efficiency of the organism’s own cellulose-degrading enzymes. This protein has the potential to be adapted for Escherichia coli and used to increase the efficiency of other multi-enzymatic reactions. By reducing the overall size of the protein and introducing a greater variety of cohesion sites, it may be possible to construct a cell surface display protein that allows significant manipulation of any appropriately modified enzymes. The project will reduce the size of the scaffolding protein and develop an anchoring protein that is compatible with the cell surface of E. coli. In the future, it may be possible to produce a collection of Bio-Brick parts that would allow teams to make adjustments to the arrangement and concentration of enzymatic subunits. This would not only increase the efficiency of multi-enzyme reactions, but also allow teams to better understand and characterize their parts.</p>
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<p>There are a plethora of enzymes that occur in the natural world which perform reactions that could be immensely useful to humans. Unfortunately, the efficiency of some of these reactions may render their applications logistically unrealistic. The cellulosome scaffolding protein produced by Clostridium thermocellum has been shown to significantly increase the efficiency of cellulose degradation. The scaffolding protein can be reduced in size and adapted for the cell surface of Escherichia coli. Different cohesion sites on the new cell surface display protein can also be introduced to allow for attachment of desired enzymes. Future applications would include producing a collection of distinct versions of the scaffolding protein for unique arrangements and concentrations of enzymes, enabling construction of an extra-cellular assembly line for a variety of multi-enzymatic reactions. This would lay the foundation for making previously infeasible applications of reactions possible through increased efficiency.</p>
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<img src="https://static.igem.org/mediawiki/2012/6/64/Missouri_Miners_Cohesin_complex.png" alt="Cohesin Complex"/>
<img src="https://static.igem.org/mediawiki/2012/6/64/Missouri_Miners_Cohesin_complex.png" alt="Cohesin Complex"/>
<p>22. Adams JJ, Currie MA, Ali S, Bayer EA, Jia Z, and Smith SP. Insights into higher-order organization of the cellulosome revealed by a dissect-and-build approach: crystal structure of interacting Clostridium thermocellum multimodular components. J Mol Biol 2010 Mar 5; 396(4) 833-9. doi:10.1016/j.jmb.2010.01.015 pmid:20070943. PubMed HubMed [cellulosome7]</p>
<p>22. Adams JJ, Currie MA, Ali S, Bayer EA, Jia Z, and Smith SP. Insights into higher-order organization of the cellulosome revealed by a dissect-and-build approach: crystal structure of interacting Clostridium thermocellum multimodular components. J Mol Biol 2010 Mar 5; 396(4) 833-9. doi:10.1016/j.jmb.2010.01.015 pmid:20070943. PubMed HubMed [cellulosome7]</p>
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Revision as of 00:00, 12 September 2012

Missouri Miners 2012

Adjustable Multi-Enzyme to Cell Surface Anchoring Protein

There are a plethora of enzymes that occur in the natural world which perform reactions that could be immensely useful to humans. Unfortunately, the efficiency of some of these reactions may render their applications logistically unrealistic. The cellulosome scaffolding protein produced by Clostridium thermocellum has been shown to significantly increase the efficiency of cellulose degradation. The scaffolding protein can be reduced in size and adapted for the cell surface of Escherichia coli. Different cohesion sites on the new cell surface display protein can also be introduced to allow for attachment of desired enzymes. Future applications would include producing a collection of distinct versions of the scaffolding protein for unique arrangements and concentrations of enzymes, enabling construction of an extra-cellular assembly line for a variety of multi-enzymatic reactions. This would lay the foundation for making previously infeasible applications of reactions possible through increased efficiency.


Cohesin Complex

22. Adams JJ, Currie MA, Ali S, Bayer EA, Jia Z, and Smith SP. Insights into higher-order organization of the cellulosome revealed by a dissect-and-build approach: crystal structure of interacting Clostridium thermocellum multimodular components. J Mol Biol 2010 Mar 5; 396(4) 833-9. doi:10.1016/j.jmb.2010.01.015 pmid:20070943. PubMed HubMed [cellulosome7]