Team:Edinburgh/Bacterial

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<span style="color:ivory;">Throughout this wiki there are words in <b>bold</b> that indicate a relevance to <b>human aspects</b>. It will become obvious that <b>human aspects</b> are a part of almost everything in <b>iGEM</b>.</span>
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Revision as of 21:52, 24 October 2010







Bacterial BRIDGEs


Communication via light.



Our Project



Figure 3: Normalised absorbance spectra of:
a. the lov2 domain of Avena sativa with bound FMN (adapted from Schüttrigkeit et al., 2003).
b. Green light absorbing form of cyanobacteriochrome CcaS from Synechocystis sp. PCC 6803. Adapted from Hirose et al, 2008.
c. Red light absorbing form of phytochrome Cph1-PCB adduct, from Synechocystis sp. PCC 6803. Adapted from Gambetta and Lagarias (2001).
Note that the relative absorbance of each spectrum is normalised to one.


The response of light receptors Cph8, lovTAP and our green light receptor to different wavelengths of light have not been measured. The absorbance spectra of the light sensitive proteins might not exactly mirror their response to light, but should give us a good idea until they are characterized.

In lovTAP, the light sensitive domain of the protein is the lov2 domain from the Avena sativa blue light receptor phototropin. This binds flavin mononucleotide (FMN) which is its co factor. Schüttrigkeit et al. (2003) measured the absorbance of the wild type lov2 bound to FMN (see Figure 3). Since this is the active part of lovTAP, we expect our blue light receptor to have a similar response in vivo. The red light absorbing form of Cph1 is what responds to red light in Cph8. The absorbance of Cph1 was measured by Gambetta and lagarias (2001). Similarly, the absorbance of the green light absorbing form of CcaS, which we are planning on using in our green light receptor, was measured by Hirose et al. (2008).



Throughout this wiki there are words in bold that indicate a relevance to human aspects. It will become obvious that human aspects are a part of almost everything in iGEM.