Difference between revisions of "Giant Jamboree/Abstracts"
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<div class='column half_size'> <h2>Aachen</h2> <p> <b> Region: </b>Europe - Germany<br><b>Section: </b>Overgraduate<br> <b>Track: </b>Diagnostics<br><b>Poster: </b>Zone 5 - #302 - Saturday - Session K & L - 6:45 PM - 8:15 PM<br><b> Presentation: </b>Saturday - Room304 - 4:45 PM - 5:15 PM</p> | <div class='column half_size'> <h2>Aachen</h2> <p> <b> Region: </b>Europe - Germany<br><b>Section: </b>Overgraduate<br> <b>Track: </b>Diagnostics<br><b>Poster: </b>Zone 5 - #302 - Saturday - Session K & L - 6:45 PM - 8:15 PM<br><b> Presentation: </b>Saturday - Room304 - 4:45 PM - 5:15 PM</p> | ||
| − | <a href="" | + | <p><a href=""> Melasense </a></p> |
<p> | <p> | ||
We plan on developing a melatonin biosensor. Our approach for the biosensor is to genetically modify Saccharomyces cerevisiae by integrating a highly specific human melatonin receptor into the cells. Melatonin has a high membrane permeability which permits us to use the nuclear retinoid z receptor (RZR) which is directly regulating gene expression. We express the RZR as a fusion-protein with the recognition sequence of the human estrogen receptor alpha (ERα). When melatonin is bound, the modified receptor binds to the estrogen receptor responsive element (ERE) and as a consequence regulate expression of firefly luciferase reporter genes. In our second approach, we will use the membrane-receptor MT1 for our biosensor. When melatonin binds to the G protein-coupled receptor, β-arrestins can be recruited. This mechanism allows us to use an enzyme fragment complementation assay based on two fusion-proteins. | We plan on developing a melatonin biosensor. Our approach for the biosensor is to genetically modify Saccharomyces cerevisiae by integrating a highly specific human melatonin receptor into the cells. Melatonin has a high membrane permeability which permits us to use the nuclear retinoid z receptor (RZR) which is directly regulating gene expression. We express the RZR as a fusion-protein with the recognition sequence of the human estrogen receptor alpha (ERα). When melatonin is bound, the modified receptor binds to the estrogen receptor responsive element (ERE) and as a consequence regulate expression of firefly luciferase reporter genes. In our second approach, we will use the membrane-receptor MT1 for our biosensor. When melatonin binds to the G protein-coupled receptor, β-arrestins can be recruited. This mechanism allows us to use an enzyme fragment complementation assay based on two fusion-proteins. | ||
Revision as of 16:10, 2 October 2018
ABSTRACTS
Aachen
Region: Europe - Germany
Section: Overgraduate
Track: Diagnostics
Poster: Zone 5 - #302 - Saturday - Session K & L - 6:45 PM - 8:15 PM
Presentation: Saturday - Room304 - 4:45 PM - 5:15 PM
We plan on developing a melatonin biosensor. Our approach for the biosensor is to genetically modify Saccharomyces cerevisiae by integrating a highly specific human melatonin receptor into the cells. Melatonin has a high membrane permeability which permits us to use the nuclear retinoid z receptor (RZR) which is directly regulating gene expression. We express the RZR as a fusion-protein with the recognition sequence of the human estrogen receptor alpha (ERα). When melatonin is bound, the modified receptor binds to the estrogen receptor responsive element (ERE) and as a consequence regulate expression of firefly luciferase reporter genes. In our second approach, we will use the membrane-receptor MT1 for our biosensor. When melatonin binds to the G protein-coupled receptor, β-arrestins can be recruited. This mechanism allows us to use an enzyme fragment complementation assay based on two fusion-proteins.
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