Part:BBa_K1733002
PYL dimerization domain
The part contains PYL (pyrabactin resistance-like), which is a dimerizable protein domain that will bind with with the ABI dimerization domain in the presence of the abscisic acid inducer. 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 abscisic acid. We were therefore able to regulate protein activity by taking advantage of these dimerization domains.
The ABI and PYL dimerization domains are found in plants. 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 and Phic31 protein ands 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 afterwards. We were able to characterize some split sites as functional, as we regained protein activity after inducing dimerization.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 282
Illegal XhoI site found at 269 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 325
- 1000COMPATIBLE WITH RFC[1000]
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