Difference between revisions of "Team:LambertGA/Description"

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<h5>Project Description</h5>
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<h5>2016 Project Description:</h5>
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Project description:
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In the latter half of the 20th Century, biologists were primarily concerned with how proteins were produced. However, so much attention was paid to the nature of the central dogma that many scientists neglected the nature of how proteins were degraded. In fact, the discovery of the lysosome by Christian de Duve in the early 1950s led many scientists to the assumption that the lysosome was the only source of protein degradation in the cell; they failed to even entertain the possibility of non-lysosomal proteolysis. With this in mind, the 2016 Lambert iGEM Team’s project revolves around the degradation of proteins through non-lysosomal processes.
 
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Coming Soon!
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A class of ATP dependent proteins (ATPases) known as ATPases Associated with Diverse Cellular Activities (AAA+) are involved in processes as diverse as protein unfolding, degradation, peroxisome biogenesis, and bacteriochlorophyll synthesis. (Cooper) This class of proteins involves a well known proteolysis mechanism known as ClpXP in which ClpX unfolds and translocates a tagged protein into a sequestered proteolytic compartment in ClpP. (Baker) To further characterize this system, our team has devised an inducible genetic construct in which ClpXP will degrade a chromoprotein upon induction. The data will be quantified with the help of a device that can capture the strength of the light reflected by the chromoprotein before, during, and after induction. Ultimately, the main goal of our project is to measure the relative strength of degradation of a chromoprotein and consequently further characterize a well known protease mechanism.
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<p>References:</p>
 
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<li>http://www.nature.com/cdd/journal/v12/n9/full/4401692a.html</li>
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<li>http://www.ncbi.nlm.nih.gov/books/NBK9957/</li>
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<li>http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3209554/</li>
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<li>http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2643927/</li>
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Revision as of 12:16, 12 August 2016

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2016 Project Description:

In the latter half of the 20th Century, biologists were primarily concerned with how proteins were produced. However, so much attention was paid to the nature of the central dogma that many scientists neglected the nature of how proteins were degraded. In fact, the discovery of the lysosome by Christian de Duve in the early 1950s led many scientists to the assumption that the lysosome was the only source of protein degradation in the cell; they failed to even entertain the possibility of non-lysosomal proteolysis. With this in mind, the 2016 Lambert iGEM Team’s project revolves around the degradation of proteins through non-lysosomal processes.

A class of ATP dependent proteins (ATPases) known as ATPases Associated with Diverse Cellular Activities (AAA+) are involved in processes as diverse as protein unfolding, degradation, peroxisome biogenesis, and bacteriochlorophyll synthesis. (Cooper) This class of proteins involves a well known proteolysis mechanism known as ClpXP in which ClpX unfolds and translocates a tagged protein into a sequestered proteolytic compartment in ClpP. (Baker) To further characterize this system, our team has devised an inducible genetic construct in which ClpXP will degrade a chromoprotein upon induction. The data will be quantified with the help of a device that can capture the strength of the light reflected by the chromoprotein before, during, and after induction. Ultimately, the main goal of our project is to measure the relative strength of degradation of a chromoprotein and consequently further characterize a well known protease mechanism.

References:

  • http://www.nature.com/cdd/journal/v12/n9/full/4401692a.html
  • http://www.ncbi.nlm.nih.gov/books/NBK9957/
  • http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3209554/
  • http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2643927/
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