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<h2 style="font-color:#000000; margin-left:50px;">Developing conditionally dimerizable split protein systems for genetic logic and genome editing applications </h2>
  
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<p style="padding-bottom:50px;">The field of synthetic biology seeks to engineer desirable cellular functionalities by developing molecular technologies that enable precise genetic manipulation. A promising solution is to reliably control proteins that naturally execute genetic modifications. Current strategies to regulate activity of such proteins primarily rely on modulating protein expression level through transcriptional control; however, these methods are susceptible to slow response and leaky expression. In contrast, strategies that exploit post-translational regulation of activity, such as conditional dimerization of split protein halves, have been demonstrated to bypass these limitations. Here, we compare the relative efficiency of previously characterized dimerization domains in regulating activities of three important genetic manipulation proteins - integrases and recombination directionality factors for genetic logic applications, and saCas9 for in vivo genome editing applications. We also establish guidelines to rationally identify promising protein split sites. Our characterization of these systems in mammalian cells ultimately paves way for important biomedical applications.</p>
  
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<td><center><a href="https://2015.igem.org/Team:BostonU/Temporal_Control"><img style="height:85%; width:85%;" src="https://static.igem.org/mediawiki/2015/thumb/9/99/Active_and_inactive_protein.png/800px-Active_and_inactive_protein.png" /></a><center></td>
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<td><h3 align="center" style="padding-bottom:50px;">Controlling Protein Activity</h3></td>
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<td><h3 align="center" style="padding-bottom:50px;">Controlling Integrases and RDFs</h3></td>
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<td><h3 align="center" style="padding-bottom:50px;">Controlling saCas9</h3></td>
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  <h1 id="sitename"><a href="https://2015.igem.org/Team:BostonU/Home">Boston University IGEM 2015  </a></h1>
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            <li class="active"><a href="https://2015.igem.org/Team:BostonU/Home">Home</a></li>
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<li><a href="https://2015.igem.org/Team:BostonU/Team">Team</a></li>
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<td><h3 align="center">Mammalian Synthetic Biology</h3></td>
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<td><h3 align="center">Education and Outreach</h3></td>
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<br><br><br><br><br><br><br><br>
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<h4 style="font-size:25px; text-align:center;">iGEM Jamboree 2015 Results</h4>
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<ol style="font-size:23px;text-align:center">Medal Received: Gold.<br>Nominated for Best Foundational Advance Project</li>
  
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<h2>Welcome to Our Project !</h2>
 
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    The goal of our team this summer is to create an efficient and widely applicable workflow for splitting proteins. By splitting proteins and fusing each half to a drug-inducible domain, scientists can gain temporal control over protein expression. Using our workflow, the proteins will be translated into two inert halves that are each fused to domains that bind in the presence of an inducer drug. By introducing the drug into the system, the two inert protein halves will come together and for a fully functioning protein. In this way, scientists can further increase their control over protein function. The two types of proteins we will be testing our workflow on are the large serine integrase family and saCAS9. These proteins harness powerful mechanisms that have significant applications in the future of synthetic biology. By using our workflow, we hope to increase scientists understanding of these proteins and also provide a mechanism for increasing temporal control.
 
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<p>Copyright Boston Unversity IGEM &copy; 2015  <a href="#"></a></p>
 
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Latest revision as of 20:30, 3 October 2015

Home

Developing conditionally dimerizable split protein systems for genetic logic and genome editing applications

The field of synthetic biology seeks to engineer desirable cellular functionalities by developing molecular technologies that enable precise genetic manipulation. A promising solution is to reliably control proteins that naturally execute genetic modifications. Current strategies to regulate activity of such proteins primarily rely on modulating protein expression level through transcriptional control; however, these methods are susceptible to slow response and leaky expression. In contrast, strategies that exploit post-translational regulation of activity, such as conditional dimerization of split protein halves, have been demonstrated to bypass these limitations. Here, we compare the relative efficiency of previously characterized dimerization domains in regulating activities of three important genetic manipulation proteins - integrases and recombination directionality factors for genetic logic applications, and saCas9 for in vivo genome editing applications. We also establish guidelines to rationally identify promising protein split sites. Our characterization of these systems in mammalian cells ultimately paves way for important biomedical applications.

Controlling Protein Activity

Controlling Integrases and RDFs

Controlling saCas9

Mammalian Synthetic Biology

Education and Outreach

Attributions








iGEM Jamboree 2015 Results

    Medal Received: Gold.
    Nominated for Best Foundational Advance Project