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Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/17717

Title: BTB Domain Dimerization:Development of a Protein-protein Interaction Assay
Authors: Wang, Qingniao
Advisor: Prive, Gilbert
Department: Biochemistry
Keywords: BTB domain
protein-protein interaction
domain dimerziation
assay development
fluorescent protein
high throughput assay
Issue Date: 22-Sep-2009
Abstract: In the human genome, 43 BTB (Bric-à-brac, Tramtrack, and Broad Complex) containing BTB-Zinc Finger proteins have been identified, many of which are transcription factors involved in cancer and development. These BTB domains have been shown to form homodimers and heterodimers which raise DNA binding affinity and specificity for transcription factors. This project was to develop an efficient assay to systematically identify interactions between BTB domains. It combined a co-expression system, fluorescent protein tagging and Ni-NTA plate retention. It was concluded that fourteen analyzed BTB domains formed homodimers, but only certain BTB pairs formed heterodimers, such as BCL6 with Miz1 and Miz1 with RP58. To further understand the specificity of BTB domain interactions, more structural and sequence information is still needed. In conclusion, this assay provided a comprehensive detection method for BTB domain interaction mapping. The information generated provides candidates for further functional and structural studies.
URI: http://hdl.handle.net/1807/17717
Appears in Collections:Master
Department of Biochemistry - Master theses

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