The role of the NF-kappa B transcription activation domain in specific and nonspecific DNA interactions

Abstract

The transcription factor NFκB activates genes that mediate inflammation, the immune response, and cell death and survival via interactions with both DNA and co-activator proteins. NFκB dimers (p50/RelA) contain a natively folded Rel-homology domain (RHD) and an intrinsically disordered transcription activation domain (TAD). Historically, the RHD was believed to mediate DNA binding whereas the TAD was responsible for the protein-protein interactions necessary for transcription activation. Nearly all previous in vitro studies have used truncated NFκB constructs and studied the roles of these domains in isolation.