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Characterizing the Expression of Transgenic Polyglutamine Repeat Proteins in A. thaliana

Status Current
Seeking Researchers No
Start Date 11/01/2010
End Date 06/30/2011
Funding Source Undergraduate Research Grant
Funding Amount 2,000
Community Partner
Related Course
Last Updated 03/02/2011 12:05AM
Keywords polyglutamine, protein

People

Faculty
  Ben Harrison

Student Researchers
  David Nash

Abstract

Most proteins encoded by an organism's genome are beneficial and thus conserved through evolution, other proteins are actually harmful, and their expression in cells is detrimental to an organism. Proteins containing long tracts of consecutive glutamine amino acids (polyglutamine) tend to aggregate in large clusters in cells of mammals, invertebrates, fungi and bacteria. In humans the aggregation of polyglutamine proteins is thought to underlie the pathology of several neurodegenerative diseases, Huntington's being the most common. It is thought that polyglutamine aggregates challenge the capacity of a cell's protein folding and turnover systems, which are normally required to maintain the proper function of many important proteins. When these systems are pre-occupied by aggregated proteins, many cellular functions are compromised and this is thought to be the basis for the cellular toxicity associated with polyglutamine proteins. While the behavior of polyglutamine proteins has been characterized in animals, fungi and bacteria, there is currently no published information regarding their properties in the plant kingdom.

We plan to investigate the behavior of proteins containing long tracts of consecutive glutamine amino acids in plants. Our first aim is to generate transgenic plants that express fluorescent proteins fused to tracts of glutamine. These fluorescent reporters will allow us to visualize the behavior of polyglutamine proteins in living plant cells. We will generate plants that express a series of glutamine tract lengths, allowing us to test the hypothesis that proteins containing longer tracts of glutamine are more prone to aggregate. Our second aim is to characterize the expression of the fluorescent polyglutamine reporters in our transgenic plants. This will include a test of our hypothesis that predicts that polyglutamine proteins will aggregate, as well as a critical verification that our reporters are expressing the intended reporter proteins. Importantly our experimental design is such that we can interpret several possible outcomes, such as the lack of aggregation of polyglutamine proteins in plant cells, and each result has biological significance.

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