Team:ETH Zurich/LovTAP

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Phototropin is a plant blue-light receptor, with a flavin mononucleotide (FMN) cofactor and  conserved cysteine residues responsible for the conformation change upon blue-light exposure<span class='eth_reference'>[Christie1999]</span>. The LovTap fusion makes use of this conformational change.  In the dark state the LovTap is not able to bind to DNA. After light activation the deformation of the TrpR domain is reversed and TrpR is able to bind to the ''trp'' operon <span class='eth_reference'>[Strickland2008]</span>.  
Phototropin is a plant blue-light receptor, with a flavin mononucleotide (FMN) cofactor and  conserved cysteine residues responsible for the conformation change upon blue-light exposure<span class='eth_reference'>[Christie1999]</span>. The LovTap fusion makes use of this conformational change.  In the dark state the LovTap is not able to bind to DNA. After light activation the deformation of the TrpR domain is reversed and TrpR is able to bind to the ''trp'' operon <span class='eth_reference'>[Strickland2008]</span>.  
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We are using the LovTap construct to be able to calculate the intensity of the UV light in combination with our UV-B sensor UVR8. Also we are using it in our duplexer as an input signal for blue light.
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We are using the LovTap construct to be able to calculate the intensity of the UV light in combination with our UV-B sensor UVR8. Also we are using it in our decoder as an input signal for blue light.
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Revision as of 21:41, 26 September 2012

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LovTap

Figure: The figure shows in blue the Lov2 domain, in yellow the TrpR and in dark blue the linker helix.

LovTap is a protein fusion of the LOV2 domain from Avena sativa phototropin1 and trp repressor from E.coli.

Phototropin is a plant blue-light receptor, with a flavin mononucleotide (FMN) cofactor and  conserved cysteine residues responsible for the conformation change upon blue-light exposure[Christie1999]. The LovTap fusion makes use of this conformational change.  In the dark state the LovTap is not able to bind to DNA. After light activation the deformation of the TrpR domain is reversed and TrpR is able to bind to the trp operon [Strickland2008].  

We are using the LovTap construct to be able to calculate the intensity of the UV light in combination with our UV-B sensor UVR8. Also we are using it in our decoder as an input signal for blue light.



References

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