Team:Bonn

From 2013.igem.org

(Difference between revisions)
Line 54: Line 54:
       <div id="page-top-slideshow">
       <div id="page-top-slideshow">
       <div id="page-top-intro" class="page-top-slide">
       <div id="page-top-intro" class="page-top-slide">
-
<img src="https://static.igem.org/mediawiki/2013/1/1f/Bonn_Logo_Batch.png" height="250px" style="float:left">
+
        <img src="https://static.igem.org/mediawiki/2013/1/1f/Bonn_Logo_Batch.png" height="250px" style="float:left">
-
<div style="padding-top:50px;width:600px;">Regulating protein activity is important throughout lifescience research. Even though there are several systems available for regulation of proteins all suffer from certain disadvantages. </br>
+
        <div style="padding-top:50px;width:600px;">
-
<span style="font-style:italic">Aiming to overcome all of these drawbacks we engineer a novel system for light dependend regulation of protein degradation resulting in a rapid change of protein activity.  
+
          Regulating protein activity is important throughout lifescience research. Even though there are several  
-
Our system can be not only of great importance for fundamental science to investigate protein function but also for accurate control of bioreactors and biological machines.</span> </div>
+
          systems available for regulation of proteins all suffer from certain disadvantages. </br>
-
      </div>
+
          <span style="font-style:italic">Aiming to overcome all of these drawbacks we engineer a novel system for  
-
      <div id="page-top-pic" class="page-top-slide">
+
          light dependend regulation of protein degradation resulting in a rapid change of protein activity.  
-
        <img src="https://static.igem.org/mediawiki/2013/f/f7/IGEM_project_LightProtAct.png" width="950px">
+
          Our system can be not only of great importance for fundamental science to investigate protein function but  
-
      </div>
+
          also for accurate control of bioreactors and biological machines.</span> </div>
 +
        </div>
 +
        <div id="page-top-pic" class="page-top-slide">
 +
          <img src="https://static.igem.org/mediawiki/2013/f/f7/IGEM_project_LightProtAct.png" width="950px">
 +
        </div>
       <div id="page-top-game" class="page-top-slide">
       <div id="page-top-game" class="page-top-slide">
         <a href="https://2013.igem.org/Team:Bonn/HP/game/"><img src="https://static.igem.org/mediawiki/2013/f/f8/Bonn_game_titelpic.png"></a>
         <a href="https://2013.igem.org/Team:Bonn/HP/game/"><img src="https://static.igem.org/mediawiki/2013/f/f8/Bonn_game_titelpic.png"></a>
Line 84: Line 88:
             Using a Split version of SspB, protein degradation is activated through heterodimerisation of both SspB  
             Using a Split version of SspB, protein degradation is activated through heterodimerisation of both SspB  
             parts.
             parts.
 +
            As a proof of principle we investigate degradation of the fluorescent reporter protein mCherry.
             To obtain light inducible degradation we use a light dependend heterodimerisation system. The light  
             To obtain light inducible degradation we use a light dependend heterodimerisation system. The light  
             sensitive part of this system is LOV2 (A. Sativa).
             sensitive part of this system is LOV2 (A. Sativa).
Line 91: Line 96:
           <div class="page-box-bottom-links">
           <div class="page-box-bottom-links">
             Find out more about </br>
             Find out more about </br>
-
             the ClpXP protease System </br>
+
             <div style="margin: 2px 0 0 5px">
-
            our Comparison of several light sensitive systems
+
              split SspB </br>
 +
              light inducible heterodimerisation </br>
 +
              our protocols </br>
 +
            </div>
           </div>
           </div>
         </div>
         </div>
Line 104: Line 112:
           Background
           Background
           </div>
           </div>
-
<div class="page-box-bottom-text">
+
          <div class="page-box-bottom-text">
-
To enable protein degradation we decided on one proteases system (ClpXP), which allows specific degradation of proteins, is highly conserved and well established.
+
            To enable protein degradation we decided on one proteases system (ClpXP), which allows specific degradation  
-
For light dependency we compared several systems to finally find the best suited one. We created a comprehensive overview of all systems making artificially light control possible so that everyone can easily choose the optimal system for his approach.
+
            of proteins, is highly conserved and well established.
-
</div>
+
            For light dependency we compared several systems to finally find the best suited one. We created a
-
<div class="page-box-bottom-links">
+
            comprehensive overview of all systems making artificially light control possible so that everyone can  
-
Find out more about </br>
+
            easily choose the optimal system for his approach.
-
the ClpXP protease System </br>
+
          </div>
-
our Comparison of several light sensitive systems
+
          <div class="page-box-bottom-links">
-
</div>
+
            Find out more about </br>
 +
            <div style="margin: 2px 0 0 5px">
 +
              the ClpXP protease System </br>
 +
              our Comparison of several light sensitive systems
 +
            </div>
 +
          </div>
         </div>
         </div>
       </div>
       </div>

Revision as of 09:24, 23 June 2013

Regulating protein activity is important throughout lifescience research. Even though there are several systems available for regulation of proteins all suffer from certain disadvantages.
Aiming to overcome all of these drawbacks we engineer a novel system for light dependend regulation of protein degradation resulting in a rapid change of protein activity. Our system can be not only of great importance for fundamental science to investigate protein function but also for accurate control of bioreactors and biological machines.
Project
Making versatile control of biological machines easily possible for everybody we engineer a system for light dependend control of protein activity per protein degradation. For protein degradation we harness the ClpXP protease system of prokaryotes. This system enables to activate degradation of a peptid tag (ssrA) fused protein upon induction with the adaptor protein SspB. Using a Split version of SspB, protein degradation is activated through heterodimerisation of both SspB parts. As a proof of principle we investigate degradation of the fluorescent reporter protein mCherry. To obtain light inducible degradation we use a light dependend heterodimerisation system. The light sensitive part of this system is LOV2 (A. Sativa). Modelling of the light dependency of protein degradation will even make simple and accurate control of protein activity for any desired level of activity possible.
Background
To enable protein degradation we decided on one proteases system (ClpXP), which allows specific degradation of proteins, is highly conserved and well established. For light dependency we compared several systems to finally find the best suited one. We created a comprehensive overview of all systems making artificially light control possible so that everyone can easily choose the optimal system for his approach.
Human Practice
Team
Sponsors

Retrieved from "http://2013.igem.org/Team:Bonn"