Team:Missouri Miners

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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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<h1 style="text-align: center;">Adjustable Multi-Enzyme to Cell Surface Anchoring Protein</h1>
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    <h2>Abstract</h2>
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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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<h2>Team History</h2>
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<p>We are the Missouri Miners from Missouri University of Science and Technology. Our team formed in 2007 with just a handful of people working on iGEM projects. Now our team has grown to nearly 30 members working hard and learning new techniques in the lab. Our team is a recognized student organization at S&T and recently became a member of the Student Design and Experiential Learning Center. Involvement in student design teams is a highly respected tradition here on our campus. Our most significant recent accomplishment was forming an extensive lab training program to verse our new members in molecular biology techniques while getting them more familiar with the lab and ready to work on future projects. The lab training program was taught in three sections by five experienced Missouri Miners iGEM student leaders. </p>
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<p>Our team is almost completely student-directed with our advisors using a "hands-off" approach. Similar to previous years, this year's project was developed by a student member of our iGEM team. This student-directed project selection and research is one of the most challenging and interesting aspects of our team; our advisors are more than willing to answer students' questions but are not directly involved in project development, project selection, or lab work. It is crucial for our team members to understand the scope and duration of projects from year to year, which allows us to manage the various stages of lab work from start to finish.<p/>
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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 03:54, 4 October 2012

Adjustable Multi-Enzyme to Cell Surface Anchoring Protein

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 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.


Team History

We are the Missouri Miners from Missouri University of Science and Technology. Our team formed in 2007 with just a handful of people working on iGEM projects. Now our team has grown to nearly 30 members working hard and learning new techniques in the lab. Our team is a recognized student organization at S&T and recently became a member of the Student Design and Experiential Learning Center. Involvement in student design teams is a highly respected tradition here on our campus. Our most significant recent accomplishment was forming an extensive lab training program to verse our new members in molecular biology techniques while getting them more familiar with the lab and ready to work on future projects. The lab training program was taught in three sections by five experienced Missouri Miners iGEM student leaders.

Our team is almost completely student-directed with our advisors using a "hands-off" approach. Similar to previous years, this year's project was developed by a student member of our iGEM team. This student-directed project selection and research is one of the most challenging and interesting aspects of our team; our advisors are more than willing to answer students' questions but are not directly involved in project development, project selection, or lab work. It is crucial for our team members to understand the scope and duration of projects from year to year, which allows us to manage the various stages of lab work from start to finish.