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Revision as of 17:10, 18 September 2015
Parts
We submitted the following three parts of our experiment to the iGEM registry:
Dimerization Domains:
These parts contain the ABI (ABA insensitive 1) and PYL (pyrabactin resistance like) protein domains that will dimerize with each other in the presence of abscisic acid. By fusing these dimerization domains to inert halves of a protein, we were able to control protein function and induce dimerization, and protein activity, with the addition of ABA (abscisic acid). We were therefore able to regulate protein activity by taking advantage of these dimerization domains.
Both ABI and PYL are found in plants1. Thus, it can be tested in mammalian cells, as the ABI-PYL-ABA system is completely orthogonal. We tested this system with our split integrases in mammalian cells.
We used this domain in our experiment to construct split protein complexes. We split the TP901-1 protein and fused the halves to ABI and PYL. We then added abscisic acid into the system to induce dimerization of the domains and the protein halves, and measured the protein activity TP901-1 afterwards. We were able to characterize some split sites as functional, as we regained the TP901-1 activity after inducing dimerization. One functional split site is shown below:
Recombination Directionality Factors:
Here is a link to our parts: Our parts page
Citations
- Liang, Fu-Sen, Ho, Wen Qi, Crabtree, Gerald R., “Engineering the ABA Stress Pathway for Regulation of Induced Proximity”, Sci Signal, 2011.