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Significance The nuclear factor kappa B (NF-κB) family of transcription factors regulates hundreds of genes in response to stress. Stress responses must be robust when needed and then completely and rapidly turned off. A family of inhibitor proteins, the IκBs, is responsible for turning off NF-κBs. Our study shows that IκBα turns off NF-κB(RelA/p50) by rapidly binding to the DNA-bound NF-κB, forming a transient ternary complex. The ternary complex lasts for only milliseconds before the DNA dissociates from the complex. The resulting IκBα–NF-κB complex is extremely stable and cannot be dissociated. Our study shows how the macromolecular interactions of IκBα are precisely tuned to efficiently and irreversibly turn off NF-κB transcriptional activity.

Direct observation of a transient ternary complex during IκBα-mediated dissociation of NF-κB from DNA