Difference between revisions of "Team:Waterloo"
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| − | + | <h2 id="caption">OFF to pri<span class="swapper0">ON</span></h2><br> | |
| + | <h4 id="title">Using stop codon read-through and CRISPR to explore <i>S. cerevisiae</i> prion mechanisms </h1> | ||
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| − | <h3 class="pan-text"> <span class="pan-background"> | + | <h3 class="pan-text"> <span class="pan-background">Furthering the advancement of research into prions and neurodegenerative diseases |
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| − | <div><img src="https://static.igem.org/mediawiki/2016/ | + | |
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| + | <div class="col-md-4 center"><img class="tsc1" style="width: 15vw" src="https://static.igem.org/mediawiki/2016/0/01/T--Waterloo--Trigger_landing.png" > | ||
| + | <h4 id="texticles1"> We initiate a [PSI+] response in S. cerevisiae using a plasmid that will overexpress Sup35-NM. </h4></div> | ||
| + | <div class="col-md-4 center"><img class="tsc2" style="width: 15vw" src="https://static.igem.org/mediawiki/2016/e/e0/T--Waterloo--Signal_landing.png"> | ||
| + | <h4 id="texticles2"> We insert a premature stop codon into an N-terminal CFP tag that will be read through and fluoresce during a [PSI+] response</h4></div> | ||
| + | <div class="col-md-4 center"><img class="tsc3" style="width: 15vw" src="https://static.igem.org/mediawiki/2016/f/fe/T--Waterloo--Control_landing.png" > | ||
| + | <h4 id="texticles3">We control read through rates by choosing the location of the premature stop codon, and can therefore control protein production in [PSI+]. We use Hsp104, a chaperone protein in S. cerevisiae, to demonstrate that our set-up phenotypically responds to the stop codon readthrough. </h4> </div> | ||
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| + | <div class="pan-text"><span style="color: #F6536D">ABSTRACT</span> </div> | ||
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| + | Prions, or “zombie proteins,” are infectious agents that lead to a variety of neurodegenerative disorders (NDDs). They sicken cells by aggregating with each other and prevent proper protein folding leading to cell death from the accumulated damage. We propose a synthetic biology approach to better study prion propagation in the model organism S. cerevisiae. Our system involves inserting a premature stop codon into a protein open reading frame of interest or into dCas9 to respectively overexpress or knock-down protein levels during a [PSI+] response. We use Hsp104, a chaperone protein in S. cerevisiae, to demonstrate that our set-up phenotypically responds to the stop codon readthrough. This research is useful for continuously observing a phenotypic output during prion propagation in yeast and may have implications for helping to identify protein targets for both prevention and treatment of NDDs in the future. | ||
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Latest revision as of 23:59, 19 October 2016
OFF to priON
Using stop codon read-through and CRISPR to explore S. cerevisiae prion mechanisms
Furthering the advancement of research into prions and neurodegenerative diseases
We initiate a [PSI+] response in S. cerevisiae using a plasmid that will overexpress Sup35-NM.
We insert a premature stop codon into an N-terminal CFP tag that will be read through and fluoresce during a [PSI+] response
We control read through rates by choosing the location of the premature stop codon, and can therefore control protein production in [PSI+]. We use Hsp104, a chaperone protein in S. cerevisiae, to demonstrate that our set-up phenotypically responds to the stop codon readthrough.
ABSTRACT
Prions, or “zombie proteins,” are infectious agents that lead to a variety of neurodegenerative disorders (NDDs). They sicken cells by aggregating with each other and prevent proper protein folding leading to cell death from the accumulated damage. We propose a synthetic biology approach to better study prion propagation in the model organism S. cerevisiae. Our system involves inserting a premature stop codon into a protein open reading frame of interest or into dCas9 to respectively overexpress or knock-down protein levels during a [PSI+] response. We use Hsp104, a chaperone protein in S. cerevisiae, to demonstrate that our set-up phenotypically responds to the stop codon readthrough. This research is useful for continuously observing a phenotypic output during prion propagation in yeast and may have implications for helping to identify protein targets for both prevention and treatment of NDDs in the future.
