Team:BostonU/Temporal Control/Workflow
Overview | Current Methods | Our Workflow |
Our Workflow
There are various post-translational protein control methods that are known in the literature. Some of these include incorporation of an allosteric binding domain to disrupt protein structure and spatial sequestration of a protein to certain regions of a cell. We focused on a method known as conditional dimerization to control protein activity.
Naturally, proteins contain different domains that work together to carry out their overall function in the cell. Conditional dimerization involves splitting a protein by separately encoding both halves; this introduces physical separation of some functional domains and eliminates protein activity. Each encoded protein fragment is fused to an additional protein domain called a dimerization domain. These domains naturally bind in the presence of an inducer, which physically brings together the protein fragments to restore protein activity.
![](https://static.igem.org/mediawiki/2015/thumb/6/68/Split_protein_separated.png/795px-Split_protein_separated.png)
![](https://static.igem.org/mediawiki/2015/thumb/2/2c/Split_protein_together.png/800px-Split_protein_together.png)
Some other specific advantages of conditional dimerization include:
- It is only necessary to know the primary sequence of a protein to develop a conditional dimerization system. The protein can be split at any particular location between adjacent amino acids. Read about our modeling efforts to determine promising split locations.
- There are several natural dimerization domains that are available in the literature. Read more about our dimerization domain choices.