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THE CANDIDATE ONCOPROTEIN BCL-3 IS AN ANTAGONIST OF P50/NF-KAPPA-B-MEDIATED INHIBITION
Author(s): FRANZOSO G, BOURS V, PARK S, TOMITAYAMAGUCHI M, KELLY K, SIEBENLIST U
Source: NATURE    Volume: 359    Issue: 6393    Pages: 339-342    Published: SEP 24 1992  
Times Cited: 237     References: 35     
Abstract: THE candidate oncogene bcl-3 was discovered as a translocation into the immunoglobulin alpha-locus 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 I-kappa-B proteins in which the ankyrin repeat domain is thought to be directly involved in inhibition of NF-kappa-B 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-kappa-B in vitro. Here we demonstrate that Bcl-3 can aid kappa-B site-dependent transcription in vivo by counteracting the inhibitory effects of p50/NF-kappa-B homodimers. Bcl-3 may therefore aid activation of select NF-kappa-B-regulated genes, including those of the human immunodeficiency virus.
Document Type: Article
Language: English
Addresses:
1. NIAID, IMMUNOREGULAT LAB, BETHESDA, MD 20892 USA
2. NCI, PATHOL LAB, BETHESDA, MD 20892 USA
Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW
Subject Category: Multidisciplinary Sciences
IDS Number: JP503
ISSN: 0028-0836
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