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J Biol Chem, Vol. 274, Issue 9, 5318-5325, February 26, 1999

IB- Enhances Transactivation by the HOXB7 Homeodomain-containing Protein

Alain Chariot, Frederic Princen, Jacques Gielen, Marie-Paule Merville, Guido Franzoso, Keith Brown, Ulrich Siebenlist, and Vincent Bours

From the  Laboratory of Medical Chemistry and Medical Oncology, Pathology, University of Liege, Sart-Tilman, 4000 Liege, Belgium and the  Laboratory of Immunoregulation, NIAID, National Institutes of Health, Bethesda, Maryland 20892

Combinatorial interactions between distinct transcription factors generate specificity in the controlled expression of target genes. In this report, we demonstrated that the HOXB7 homeodomain-containing protein, which plays a key role in development and differentiation, physically interacted in vitro with IB-, an inhibitor of NF-B activity. This interaction was mediated by the IB- ankyrin repeats and C-terminal domain as well as by the HOXB7 N-terminal domain. In transient transfection experiments, IB- markedly increased HOXB7-dependent transcription from a reporter plasmid containing a homeodomain consensus-binding sequence. This report therefore showed a novel function for IB-, namely a positive regulation of transcriptional activation by homeodomain-containing proteins.

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