Difference between revisions of "Team:Waterloo"

 
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{{Waterloo}}
 
 
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Background:
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{{Waterloo/head}}
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Prions are a specific type of protein aggregate, consisting of only one protein, and possessing the interesting characteristic of being “infectious.” Proteins in the aggregate (in an insoluble form) have a different conformation than the same protein outside of the aggregate (in a soluble form), but if the former encounter the latter, the latter will “misfold” and join the aggregate.
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Though prions were first recognized in association with infectious diseases in mammals, prion-like proteins have been found in many organisms, with examples in yeast like Sup35 being particularly well studied. These prion-like proteins can form aggregates that share most of the same physical properties as prions in mammals. Importantly, however, the presence of the aggregated form of these proteins does not seem to have a significant negative effect on a cell. This suggests that many prion-like proteins actually serve some important function. These proteins are thus deemed functional prion proteins.
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The proteins that form both disease prions and functional prions have a specific region in their amino acid sequence referred to as the prion domain. If one deletes this sequence, the proteins lose their ability to form prions. If one adds this sequence to a typical protein, then that protein will gain the ability to form prion-like aggregates; in essence, it becomes a prion protein.
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Many of these proteins decrease in function when they aggregate. For instance, Sup35 performs its function much less efficiently when aggregated. However, there is at least one functional prion that sees an increase of function upon aggregation. This protein is CPEB, the homologs of which are found in the neurons of several animals. CPEB tags certain mRNAs for translation, but it can only do this when in its aggregated form.
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The project:
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<p>Inline <strong>markdown</strong>!</p>
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It has been theorized, as well as demonstrated, that fusing the prion domain to different proteins can reduce their function when aggregates are present. However, it would be interesting to cause an increase in function upon aggregation. This is the basis for the project this year.
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<p>WATERLOO</p>
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In this project, we will fuse the prion domain of Sup35 to two halves of a fluorescent protein. If these halves come close together in the cell, they will combine and fluoresce. By inducing Sup35 aggregation in yeast, we hope to get our two fluorescent protein fragment-prion domain fusions to join the same aggregate. In the aggregate, the two fusion proteins should be brought in close proximity, giving the fluorescent protein fragments the chance to come together. This is evidence that proteins can join an aggregate while keeping their normal function, and that different proteins can be brought together in the same aggregate.
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<p>More working md?</p>
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Bringing proteins close in this way is, in theory, sufficient to increase the interaction between them. If we attach the same prion domain to two proteins that normally interact, there is a good chance that we can increase their interaction by inducing aggregation.
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A second possible way to check for the viability of protein-protein interaction in the prion is to use a technique called FRET. Basically this technique is a way to check if two fluorescent proteins are in close proximity. We would attach prion domains to two complete fluorescent proteins and get them both to join the aggregate. To give a simplified explanation, depending on the fluorescence signal we get from exciting one of the protein, we should be able to tell if it’s in close proximity to the other. As mentioned earlier, proximity of two proteins is usually sufficient to increase interaction.
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<h1> Welcome to iGEM 2017! </h1>
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<p>Your team has been approved and you are ready to start the iGEM season! </p>
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<h5>Before you start: </h5>
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<li> <a href="https://2017.igem.org/Competition">Competition Hub</a> </li>
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<li> <a href="https://2017.igem.org/Competition/Deliverables/Wiki">Wiki Requirements page</a></li>
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<nav class="navbar navbar-toggleable-md navbar-inverse bg-primary fixed-top"><a class="navbar-brand" href="https://2017.igem.org/Team:Waterloo">Waterloo</a><button class="navbar-toggler navbar-toggler-right" type="button" data-toggle="collapse" data-target="#navbarCollapse" aria-controls="navbarCollapse" aria-expanded="false" aria-label="Toggle navigation">
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            <text id="Subheadings:-Li-Euro" font-family="AvenirNext-Regular, Avenir Next" font-size="30" font-weight="normal" fill="#E8E96B">
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                <tspan x="593.905" y="112">Prion like proteins can stick</tspan>
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                <tspan x="593.905" y="153">together and form aggregates</tspan>
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            </text>
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            <text id="Subheadings:-Li-Euro" font-family="AvenirNext-Regular, Avenir Next" font-size="30" font-weight="normal" fill="#E8E96B">
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                <tspan x="17.91" y="381">Aggregates are generally thought to be</tspan>
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                <tspan x="17.91" y="422">harmful to some cells, but functional</tspan>
 +
                <tspan x="17.91" y="463">amyloid and engineered prions could be a </tspan>
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                <tspan x="17.91" y="504">useful tool in medicine, research, and</tspan>
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                <tspan x="17.91" y="545"> manufacturing</tspan>
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            </text>
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            <text id="Subheadings:-Li-Euro" font-family="AvenirNext-Regular, Avenir Next" font-size="30" font-weight="normal" fill="#E8E96B">
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                <tspan x="593.905" y="737">Functional amyloids are found in</tspan>
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                <tspan x="593.905" y="778">nature, however little is known</tspan>
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                <tspan x="593.905" y="819">about how proteins behave when</tspan>
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                <tspan x="593.905" y="860">they are in aggregates</tspan>
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            </text>
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    </g>
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</svg></p>
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<center>
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<div style="max-width: 600px; display:inline-block;">
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<img src="https://static.igem.org/mediawiki/2017/e/e5/Waterloo_splash_footer.png"></img>
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<h2>We aim to enhance the function and better understand engineered proteins in aggregates</h2>
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<a href="https://2017.igem.org/Team:Waterloo/Description"><button class="btn btn-secondary btn-large">Read more!</button></a>
 
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</div></div></div>
 
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<h5> Wiki template information </h5>
 
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<p>We have created these wiki template pages to help you get started and to help you think about how your team will be evaluated. You can find a list of all the pages tied to awards here at the <a href="https://2017.igem.org/Judging/Pages_for_Awards">Pages for awards</a> link. You must edit these pages to be evaluated for medals and awards, but ultimately the design, layout, style and all other elements of your team wiki is up to you!</p>
 
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<h5> Editing your wiki </h5>
 
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<p>On this page you can document your project, introduce your team members, document your progress and share your iGEM experience with the rest of the world! </p>
 
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<p> <a href="https://2017.igem.org/wiki/index.php?title=Team:Example&action=edit"> </a>Use WikiTools - Edit in the black menu bar to edit this page</p>
 
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<h5>Tips</h5>
 
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<p>This wiki will be your team’s first interaction with the rest of the world, so here are a few tips to help you get started: </p>
 
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<ul>
 
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<li>State your accomplishments! Tell people what you have achieved from the start. </li>
 
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<li>Be clear about what you are doing and how you plan to do this.</li>
 
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<li>You have a global audience! Consider the different backgrounds that your users come from.</li>
 
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<li>Make sure information is easy to find; nothing should be more than 3 clicks away.  </li>
 
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<li>Avoid using very small fonts and low contrast colors; information should be easy to read.  </li>
 
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<li>Start documenting your project as early as possible; don’t leave anything to the last minute before the Wiki Freeze. For a complete list of deadlines visit the <a href="https://2017.igem.org/Calendar">iGEM 2017 calendar</a> </li>
 
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<li>Have lots of fun! </li>
 
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<h5>Inspiration</h5>
 
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<p> You can also view other team wikis for inspiration! Here are some examples:</p>
 
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<ul>
 
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<li> <a href="https://2014.igem.org/Team:SDU-Denmark/"> 2014 SDU Denmark </a> </li>
 
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<li> <a href="https://2014.igem.org/Team:Aalto-Helsinki">2014 Aalto-Helsinki</a> </li>
 
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<li> <a href="https://2014.igem.org/Team:LMU-Munich">2014 LMU-Munich</a> </li>
 
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<li> <a href="https://2014.igem.org/Team:Michigan"> 2014 Michigan</a></li>
 
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<li> <a href="https://2014.igem.org/Team:ITESM-Guadalajara">2014 ITESM-Guadalajara </a></li>
 
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<li> <a href="https://2014.igem.org/Team:SCU-China"> 2014 SCU-China </a></li>
 
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<h5> Uploading pictures and files </h5>
 
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<p> You can upload your pictures and files to the iGEM 2017 server. Remember to keep all your pictures and files within your team's namespace or at least include your team's name in the file name. <br />
 
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When you upload, set the "Destination Filename" to <br><code>T--YourOfficialTeamName--NameOfFile.jpg</code>. (If you don't do this, someone else might upload a different file with the same "Destination Filename", and your file would be erased!)<br><br>
 
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<a href="https://2017.igem.org/Special:Upload">
 
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UPLOAD FILES
 
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{{Waterloo/footer}}

Latest revision as of 02:00, 2 November 2017

Functional Amyloid as a Biological Tool

Created with Sketch. Prion like proteins can stick together and form aggregates Aggregates are generally thought to be harmful to some cells, but functional amyloid and engineered prions could be a useful tool in medicine, research, and manufacturing Functional amyloids are found in nature, however little is known about how proteins behave when they are in aggregates

We aim to enhance the function and better understand engineered proteins in aggregates

Waterloo iGEM 2017

© 2017 Waterloo iGEM