Date of Award
Master of Science (MS)
Dr. Aimin Liu
Dr. David Wilson
Dr. Donald Hamelberg
The transcription factor NF-κB interacts with many other co-regulator proteins that modulate its binding and transcriptional activity. One of these co-regulators, Pirin, is an iron-dependent metalloprotein that has been shown to enhance the DNA binding of NF-κB homodimers. Here, we characterize the interactions between Pirin and its known NF-κB binding partners and examined the role of Bcl-3, a protein that is required for Pirin’s interaction with p50. In addition, we use site-directed mutagenesis to alter conserved residues within Pirin’s metal binding environment and observed how it affected the DNA binding and conformation of the Pirin-NF-κB complex. These studies show that, while a similar enhancing effect on DNA binding is observed, the interactions of Pirin with different NF-κB members are distinct from each other and could possibly have different physiological purposes.
Rehmani, Imran J., "Studying the DNA Binding and Conformation of Metal-Binding Site Mutations in Pirin" (2012). Chemistry Theses. Paper 53.
Available for download on Wednesday, July 16, 2014