Difference between revisions of "Team:LambertGA"

 
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<center> <h1 id="MainTitle"><b> SWITCH </b></h1>
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Micronutrient deficiency is one of the leading causes of death in the world. According to the World Health Organization (WHO), more than 2 billion people - over 30% of the world’s population - suffer from micronutrient deficiencies today. In response, healthcare providers around the world have organized research facilities to diagnose and treat micronutrient deficiency. However, diagnosing these deficiencies has proved to be extremely expensive and, in many cases, very time consuming. To address this growing concern, medical researchers and synthetic biologists are creating simple and inexpensive “biosensors” that serve as handy diagnostic tests to use in the field to visualize micronutrient levels and determine whether the patient and population in general are lacking critical micronutrients in their diet. Despite these benefits, this versatile tool often yields inaccurate results, potentially leading to faulty diagnosis and the endangerment of an entire community.
  
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With this in mind, the 2016 Lambert iGEM Team has focused primarily on enhancing existing biosensors and aiding in the diagnosis of micronutrient deficiencies throughout the world. We studied protein degradation and devised a “switch” to prevent the overexpression of specific reporters in biosensors in order to fine-tune biosensor accuracy. By using SsrA degradation tags, we characterized ClpXP, a protease involved in non-lysosomal proteolysis in many prokaryotes, to quantify the relative strength of degradation in GFP and purple chromoproteins.
  
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<h2> Silver Medal </h2><br>
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<p>Protein degradation has two main methods: the more well-known lysosomal processes and the newly discovered non-lysosomal mechanisms.  Our 2016 project, SWITCH, is focusing on a specific non-lysosomal mechanism called ClpXP.  The system is composed of two subunits - ClpX, which linearizes the protein marked with a degradation tag, and ClpP, which degrades the protein into component amino acids. We have created an inducible genetic construct to regulate the transcription of ClpXP, giving the ability to characterize the degradation of chromoproteins; we have quantified the data using light reflection from the chromoprotein tsPurple using a prototype lightbox/camera.  The further characterization of protein degradation is necessary for the precision and control necessary for the administration of medicines and the function of biosensors, specifically Georgia Tech’s Zinc biosensor.</p>
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<p>The concentration of proteins in a cell is determined by both the amount synthesized and the amount naturally degraded. Thus, protein degradation is a crucial aspect of maintaining intramolecular equilibrium. A class of ATPases known as AAA+ Proteins contains a well-known proteolysis mechanism known as ClpXP in which the ClpX piece unfolds and translocates a tagged protein into a sequestered proteolytic compartment in ClpP. The tagged, linearized polypeptide is then degraded into free amino acids.</p>
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Latest revision as of 20:25, 11 November 2016

Characterization of Nonlysosomal Proteolysis


Micronutrient deficiency is one of the leading causes of death in the world. According to the World Health Organization (WHO), more than 2 billion people - over 30% of the world’s population - suffer from micronutrient deficiencies today. In response, healthcare providers around the world have organized research facilities to diagnose and treat micronutrient deficiency. However, diagnosing these deficiencies has proved to be extremely expensive and, in many cases, very time consuming. To address this growing concern, medical researchers and synthetic biologists are creating simple and inexpensive “biosensors” that serve as handy diagnostic tests to use in the field to visualize micronutrient levels and determine whether the patient and population in general are lacking critical micronutrients in their diet. Despite these benefits, this versatile tool often yields inaccurate results, potentially leading to faulty diagnosis and the endangerment of an entire community.

With this in mind, the 2016 Lambert iGEM Team has focused primarily on enhancing existing biosensors and aiding in the diagnosis of micronutrient deficiencies throughout the world. We studied protein degradation and devised a “switch” to prevent the overexpression of specific reporters in biosensors in order to fine-tune biosensor accuracy. By using SsrA degradation tags, we characterized ClpXP, a protease involved in non-lysosomal proteolysis in many prokaryotes, to quantify the relative strength of degradation in GFP and purple chromoproteins.




Silver Medal


Nominated for Best Wiki


Nominated for Best Poster