The NF-kappaB family of transcription factors is renowned for its crucial role in immune response. While NF-kappaB is primarily recognized as a transcription activator, it also serves as a transcription repressor for specific genes. In my presentation, I will delve into the insights obtained regarding the molecular mechanism of repression by the NF-kappaB p50 subunit, utilizing NMR spectroscopy as a powerful tool.
Our research focuses on characterizing the 73.1 kDa homodimer of the NF-kappaB p50 subunit, both in its free and in DNA-bound state. Using chiefly NMR spectroscopy, our study reveals that in the absence of nucleic acids, the two constituent domains of the NF-kappaB p50 subunit, namely the DNA recognizing N-terminal domain and the dimerization domain, exist as structurally independent entities. The findings from our study provide valuable insights into a potential mechanism underlying the release of NF-kappaB from the p50-repressor complex.