Abstract

The nBmp2 protein was first identified in a DNA affinity chromatography/mass spectrometry screen designed to detect proteins that interact with a cartilage-specific enhancer element (called D/E) from the type XI collagen gene Col11a2. The transcription factor SOX9, a protein from the Sox (SRY-related HMG box) family, binds to and activates gene expression from this enhancer. nBmp2 has no transcriptional activity of its own on this enhancer, but when co-transfected with SOX9 it increases SOX9's activation of D/E nearly 2-fold. SOX9 also activates cartilage-specific enhancer elements from the Col2a1, Col27a1, and Col9a1 genes. The purpose of this project was to determine 1) whether nBmp2 similarly effects SOX9-dependent expression from these enhancers, and 2) whether it does so by binding (either directly or indirectly) to the Col2a1, Col27a1, and Col9a1 enhancers. The work described in this thesis has shown that nBmp2 increases luciferase levels produced from three enhancer/reporter plasmids, but it does so without binding directly to the enhancers. This work has opened up a new area of exploration into the function of the novel protein nBmp2 to examine its potential effects on a variety of different gene regulatory processes.

Degree

College and Department

Life Sciences; Microbiology and Molecular Biology

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