Difference between revisions of "Team:Washington/Parts"

Line 156: Line 156:
 
<html>
 
<html>
 
We also have an automatically generated <a href="http://partsregistry.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2015&group=Washington">Team Parts</a> page.</html>
 
We also have an automatically generated <a href="http://partsregistry.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2015&group=Washington">Team Parts</a> page.</html>
 +
 +
                    <h2>Auxin</h2>
 +
 +
<p align = "justify"> This part, called AFB2, is an F-box protein that binds the common plant hormone auxin. F-box proteins contain an F-box domain that mediates degradation of other proteins by recognizing substrates for ubiquitination. </p>
 +
 +
<p align = "justify"> In our system, a dCas9-degron-repressor complex represses expression of lacZ. In the presence of auxin, the F-box protein and the presence of auxin, the AFB2 binds to auxin and auxin also binds to a degron; the F-box protein then recruits the ubiquitin ligase to degrade the dCas9-degron-repressor complex. When this occurs, lacZ is no longer repressed and production of beta galactosidase occurs. Beta galactosidase acts as a reporter for the presence of auxin. </p>
  
 
       <h2>Apatazyme</h2>
 
       <h2>Apatazyme</h2>

Revision as of 03:32, 19 September 2015



Biobricks

Parts in the registry

<groupparts>iGEM015 Washington</groupparts>

We also have an automatically generated Team Parts page.

Auxin

This part, called AFB2, is an F-box protein that binds the common plant hormone auxin. F-box proteins contain an F-box domain that mediates degradation of other proteins by recognizing substrates for ubiquitination.

In our system, a dCas9-degron-repressor complex represses expression of lacZ. In the presence of auxin, the F-box protein and the presence of auxin, the AFB2 binds to auxin and auxin also binds to a degron; the F-box protein then recruits the ubiquitin ligase to degrade the dCas9-degron-repressor complex. When this occurs, lacZ is no longer repressed and production of beta galactosidase occurs. Beta galactosidase acts as a reporter for the presence of auxin.

Apatazyme

yeVenus-TheoA; Coding sequence for enhanced YFP and theophylline-sensative aptazyme

<a href="http://parts.igem.org/Part:BBa_K1711001">http://parts.igem.org/Part:BBa_K1711001</a>

The part contains the coding sequence for yeast enhanced yellow fluorescent protein (yeVenus), linked to it is a gene for a theophylline sensitive riboswitch aptazyme. The aptazyme portion of the transcript self-cleaves in the absence of theophylline and no YFP should be produced. The theophylline bound state stabilizes the transcript, which translates to the protein and fluorescence should be observed.

yeVenus-PEST-TheoA; Coding sequence for destabilized YFP Venus and theophylline-sensitive aptazyme

<a href="http://parts.igem.org/Part:BBa_K1711002">http://parts.igem.org/Part:BBa_K1711002</a>

This part, yeVenus-PEST-TheoA, contains the coding sequence for a hybrid protein made of yeast enhanced yellow fluorescent protein (yeVenus) fused in frame with the CDS of the PEST-rich 178 c-terminal residues of Cln2, which targets the protein for ubiquitin dependent degradation. These coding sequences are fused with a gene for a theophylline sensitive riboswitch aptazyme. The aptazyme portion of the transcript self-cleaves in the absence of theophylline and no YFP should be produced. The theophylline bound state stabilizes the transcript, which translates to the protein and fluorescence should be observed.


</div> </div> </html>