Team:Grenoble/Biology/Network

From 2012.igem.org

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The dipeptide bind to his receptor which is an engineered receptor:  
The dipeptide bind to his receptor which is an engineered receptor:  
<ul><li>the extracellular part is the extracellular part of Tap, a dipeptide receptor involved in the chemotaxism</li>
<ul><li>the extracellular part is the extracellular part of Tap, a dipeptide receptor involved in the chemotaxism</li>
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<li>the intracellular part is the intracellular part of EnvZ, an osmolarity sensor protein</li>
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<li>the intracellular part is the intracellular part of EnvZ, a kinase involved in the osmoregulation</li>
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</ul>
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Once the dipeptide is bound, the EnvZ part allows the phosphorylation of OmpR
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Once the dipeptide is bound, the EnvZ part allows the phosphorylation of OmpR, a transcriptional activator. It can now activate the pOmpC promotor
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Revision as of 21:30, 23 September 2012

iGEM Grenoble 2012

Project

Network details

Signaling module

The signaling module allows our bacterial strain to integrate the input signal = the pathogene presence.

Stapylococcus aureus secrete a protease nom de la protéase which cut a specific amino-acids sequence. This specific sequence can be used as a linker between a membrane protein and a dipeptide.
Once S. aureus is present, the linker is cut by the protease and the dipeptide is released.

The dipeptide bind to his receptor which is an engineered receptor:
  • the extracellular part is the extracellular part of Tap, a dipeptide receptor involved in the chemotaxism
  • the intracellular part is the intracellular part of EnvZ, a kinase involved in the osmoregulation

Once the dipeptide is bound, the EnvZ part allows the phosphorylation of OmpR, a transcriptional activator. It can now activate the pOmpC promotor

Amplification module