IGEM:Imperial/2010/Fast Response module: Difference between revisions
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==Idea 1== | ==Idea 1== | ||
The first idea, that seems to be feasible considering all the components, is the one below: | The first idea, that seems to be feasible considering all the components, is the one below: | ||
[[Image:OmpR system pic.jpg]] | |||
This is a bacterial two component system. On recieving of a signal, the Env Z receptor autophosphorylates. The phosphate is then passed on the respond element, a transcription factor called OmpR. OmpR is a molecule found naturally downstream of the signalling cascade from the EnvZ receptor. On phosphorylation the OmpR-P dimerise. Since each OmpR is fused with a split protease, when the OmpRs come together, the split protease (TEV) domains come together. This produces the active protease. | |||
References: | |||
*The split protease TEV: [[http://www.nature.com/nmeth/journal/v3/n12/full/nmeth967.html|Monitoring regulated protein-protein interactions using split TEV]] | |||
*The EnvZ-OmpR system: [[http://www.ncbi.nlm.nih.gov/pubmed/15979641|The response regulator OmpR oligomerizes via beta-sheets to form head-to-head dimers.]] |
Revision as of 02:42, 20 July 2010
Signalling |
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2 components systems |
logic gate |
Vibrio cholera |
Idea 1
The first idea, that seems to be feasible considering all the components, is the one below:
This is a bacterial two component system. On recieving of a signal, the Env Z receptor autophosphorylates. The phosphate is then passed on the respond element, a transcription factor called OmpR. OmpR is a molecule found naturally downstream of the signalling cascade from the EnvZ receptor. On phosphorylation the OmpR-P dimerise. Since each OmpR is fused with a split protease, when the OmpRs come together, the split protease (TEV) domains come together. This produces the active protease.
References:
- The split protease TEV: [regulated protein-protein interactions using split TEV]
- The EnvZ-OmpR system: [response regulator OmpR oligomerizes via beta-sheets to form head-to-head dimers.]