| Popis: |
The transcription factor NF-?B 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-?B homodimers. Here, we characterize the interactions between Pirin and its known NF-?B 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-?B complex. These studies show that, while a similar enhancing effect on DNA binding is observed, the interactions of Pirin with different NF-?B members are distinct from each other and could possibly have different physiological purposes. |
