ASSOCIATION BETWEEN PROTO-ONCOPROTEIN REL AND TATA-BINDING PROTEIN MEDIATES TRANSCRIPTIONAL ACTIVATION BY NF-KAPPA-B

The c-Rel protein is able to associate in vitro and in vivo with the TATA-binding protein (TBP) of the TFIID complex. Coexpression of TBP with c-Rel augments transactivation from the kappaB site in Drosophila Schneider cells. DNA-binding mutants of TBP not only fall to cooperate, but they repress transactivation by c-Rel. There may be a direct communication between kappaB enhancer binding proteins and basal transcription factors which leads to enhanced transcription.