Description: Coming up with a fancy idea is easy, however, coming up with a promising as well as feasible one is hard, harder than we imagined.Our leader encouraged every member to think about ideas, and we successfully did that. Initially, we acquired about 10 ideas and discussed each one of them. After 2 weeks, three ideas left to be further determined whether they are appropriate or not. They were: 1. Bacteria feeds on plastic 2. EEEEE(Extremely Enhanced Expessing Engineered E.coli ) 3. Prion and its aggregating 2. EEEEE(Extremely Enhanced Expessing Engineered E.coli ) Our criteria for ideas are as follow:Will our team members have fun? Is our time enough for it? Is our experiment equipment enough? Does it meet iGEM safety requirements? Is it innovative enough?We finally decided to select "Prion and its aggregating" as our project carrier. Information found is as below:In yeast cell, there is a non-Mendelian inheritance system.Figure 1: The effect of [PSIC] on Sup35 and translational termination. (A) A complex of Sup35 (see legend at bottom) and Sup45 binds ribosomes at stop codons and mediates translational termination. Sup35 is composed of two regions, a prion-determining-domain (PrD, rectangle) and a termination domain (Sup35C, sphere). In non-prion [ psi¡] strains, translational termination occurs efficiently at stop codons at the ends of open reading frames, and the completed protein is released from the ribosome.(B) In [PSIC] cells, most Sup35 proteins adopt the prion conformation and self-assemble into an aggregated, possibly amyloid structure (depicted as large cylinder). This conformational change impairs Sup35’s ability to participate in translational termination and consequently, stop codons are read through occasionally, producing proteins with a C-terminal extension.Moreover, it shows that the PrD can be modularized, which means we can combine this domain to another protein we want to make them aggregate, and even impair its function.Here is the most magical part ,not only can we make them aggregate, we can also cure our yeast by a great variety of chemical, environmental, and protein-based agents. Then these proteins will be depolymerized, and spread uniformly in the cell once again. In the first design (figure 2), we just use R9 to depolymerize the SUP35’s aggregation to allow the yeast to produce functional GFP. Then we can calculate the concentration of R9 through the fluorescent brightness. In the second design (figure 3), we build a double direction switch. In the third design (figure 4), GFP1 and GFP2 are not able to give out light separately. However, when they touch each other physically, they will reconstruct and give out light.We hope to construct a bio-reaction controller, which functions directly on protein level rather than on DNA level in advance. Such strategy is highly possible to reduce the time it takes for the controlling effect to appear, as DNA->Protein process is skipped.
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Year: 2016Visit Wiki
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Updated at: 8/9/16