Team:Missouri Miners/Test

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There are a multitude of situations in which several reactions are carried out outside the cell by a sereies of secreted enzymes to acheive the desired product. These processes can sometimes suffer decreased efficiency due to the unavoidable randomness of the enzymes involved in the given reaction. Clostridium Thermocellum utilizes an effecient and well characterized cellulosome scaffoldin molecule in conjuction with a anchoring protein to bind multiple catalytic subunits to its membrane. The subunits consists of two parts: a complete and functioning enzyme, and a docking domain which binds to one of several cohesion sites located on the cellulosome scaffoldin. There are a variety of docking sites which are compatible with a variety of cohesion sites. In C. Thermocellum, this allows multiple cellulose degrading enzymes to be optimally positioned for cellulose degredation. Our team proposes to express a modified version of a C. Thermocellum cellulosome in E. coli so that we may anchor a hybrid enzyme to the cell's surface. The hybrid enzyme will include the complete alkalane phophotase and one of the docking sites normally include in C. Thermocellum's own catalytic subunits. If the project is a sucess, it will be a step towards the standardization of cell surface enzyme anchoring and positioning of enzymes involved in multi-step processes.
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<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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<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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<img src="https://static.igem.org/mediawiki/2012/6/64/Missouri_Miners_Cohesin_complex.png" alt="Cohesin Complex"/>
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<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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Latest revision as of 17:25, 14 September 2012

Missouri Miners 2012

Abstract

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.


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]

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