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Visualization of the tissue-specific promoter activity of the genes encoding protein disulfide isomerase-7, -12 and -13 in Arabidopsis thaliana
|Title:||Visualization of the tissue-specific promoter activity of the genes encoding protein disulfide isomerase-7, -12 and -13 in Arabidopsis thaliana|
|Contributors:||Christopher, David (advisor)|
|Keywords:||Protein disulfide isomerase|
GUS reporter system
|Date Issued:||26 Sep 2014|
|Publisher:||University of Hawaii at Manoa|
|Abstract:||For proteins to properly carry out their functions, they must be folded correctly. Protein disulfide isomerases (PDIs) assist protein folding by catalyzing the formation and/or rearrangement of disulfide bonds between cysteine residues in newly- synthesized polypeptides. The goal of the project is to characterize the expression patterns of three PDI genes in the model plant, Arabidopsis thaliana. The Arabidopsis PDI (AtPDI) family consists of 13 members, the majority of which are found in the endoplasmic reticulum (ER), possess two catalytic domains, but lack transmembrane domains. In contrast, AtPDI7, AtPDI12 and AtPDI13 are unusual PDIs because they are primarily located at the Golgi apparatus, and possess two transmembrane domains and only one catalytic domain. Using the β-glucuronidase (GUS) reporter system, these three PDI genes were determined to have distinct tissue-regulated expression patterns. The AtPDI7 promoter was primarily active in developing tissues, while the AtPDI12 promoter was active in pollen, stipules, developing seeds, and the vasculature of roots. The AtPDI13 promoter activity was restricted to pollen and stipules. Interestingly, the AtPDI12 promoter was also inducible at the root tip by the plant hormone, auxin. The variable GUS staining patterns imply that there may be partial functional specificity between AtPDI7, AtPDI12, and AtPDI13. Further characterization of the tissue-specific expression of these PDIs would contribute in the understanding of how the different members of the PDI family each contribute to the process of protein folding in organisms.|
|Pages/Duration:||iii, 25 pages|
|Rights:||All UHM Honors Projects are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission from the copyright owner.|
|Appears in Collections:||
Honors Projects for Microbiology|
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