Abstract
THE candidate oncogene bcl-3 was discovered as a translocation into the immunoglobulin alphalocus in some cases of B-cell chronic lymphocytic leukaemias1. The protein Bcl-3 contains seven so-called ankyrin repeats. Similar repeat motifs are found in a number of diverse regulatory proteins but the motifs of Bcl-3 are most closely related to those found in 1κB proteins in which the ankyrin repeat domain is thought to be directly involved in inhibition of NF-κB activity. No biological function has yet been described for Bcl-3, but it was noted recently2 that Bcl-3 interferes with DNA-binding of the p50 subunit of NF-κB in vitro. Here we demonstrate that Bcl-3 can aid κB site-dependent transcription in vivo by counteracting the inhibitory effects of p50/NF-κB homodimers. Bcl-3 may therefore aid activation of select NF-κB-regulated genes, including those of the human immunodeficiency virus.
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Franzoso, G., Bours, V., Park, S. et al. The candidate oncoprotein Bcl-3 is an antagonist of pSO/NF-κB-mediated inhibition. Nature 359, 339–342 (1992). https://doi.org/10.1038/359339a0
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DOI: https://doi.org/10.1038/359339a0
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