Most nuclear factor-kappa B (NF-kappa B) inducers converge to activate the I kappa B kinase (IKK) complex, leading to NF-kappa B nuclear accumulation. However, depending on the inducer and the cell line, the subset of NF-kappa B-induced genes is different, underlining a complex regulation network. Recent findings have begun to delineate that histone and non-histone protein acetylation is involved, directly and indirectly, in controlling the duration, strength and specificity of the NF-kappa B-activating signaling pathway at multiple levels. Acetylation and deacetylation events, in combination with other post-translational protein modifications, generate an 'NF-kappa B-signaling code' and regulate NF-kappa B-dependent gene transcription in an inducer- and promoter-dependent manner. Indeed, the intricate involvement of histone acetyltransferases and histone deacetylases modulates both the NF-kappa B-signaling pathway and the transcriptional transactivation of NF-kappa B-dependent genes.