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NF-κB is a key regulator of immune gene expression in metazoans. It is currently unclear what changes occurred in NF-κB during animal evolution and what features remained conserved. To address this question, we compared the biochemical and functional properties of NF-κB proteins derived from human and the starlet sea anemone (Nematostella vectensis) in 1) a high-throughput assay of in vitro preferences for DNA sequences, 2) ChIP analysis of in vivo recruitment to the promoters of target genes, 3) a LUMIER-assisted examination of interactions with cofactors, and 4) a transactivation assay. We observed a remarkable evolutionary conservation of the DNA binding preferences of the animal NF-κB orthologs. We also show that NF-κB dimerization properties, nuclear localization signals, and binding to cytosolic IκBs are conserved. Surprisingly, the Bcl3-type nuclear IκB proteins functionally pair up only with NF-κB derived from their own species. The basis of the differential NF-κB recognition by IκB subfamilies is discussed.

Original publication

DOI

10.1074/jbc.M113.451153

Type

Journal article

Journal

J Biol Chem

Publication Date

19/04/2013

Volume

288

Pages

11546 - 11554

Keywords

Animals, Biological Evolution, Humans, NF-kappa B, Nuclear Localization Signals, Protein Multimerization, Proto-Oncogene Proteins, Sea Anemones, Species Specificity, Transcription Factors