The ankyrin repeat domains of the NF-kappa B precursor p105 and the protooncogene bcl-3 act as specific inhibitors of NF-kappa B DNA binding

摘要: Abstract The inducible pleiotropic transcription factor NF-kappa B is composed of two subunits, p50 and p65. The subunit encoded on the N-terminal half a 105-kDa open reading frame contains rel-like domain. To date, no function has been described for C-terminal portion. We show here that p105, when expressed as separate molecule, binds to can rapidly disrupt protein-DNA complexes or native B. Deletion analysis this precursor-derived inhibitor activity indicated domain containing ankyrin-like repeats necessary inhibition. protooncogene bcl-3, which seven ankyrin repeats, equally inhibit DNA binding. These observations identify bcl-3 an strongly suggest in these factors are involved protein-protein interactions with p50. Comparison other repeat-containing proteins suggests subclass acts regulators factors.