Abstract
The candidate oncogene bcl-3 was discovered as a translocation into the immunoglobulin alpha-locus in some cases of B-cell chronic lymphocytic leukaemias. 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 recently 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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Ankyrins / genetics
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B-Cell Lymphoma 3 Protein
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Cell Line
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Cell Nucleus / metabolism
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Chloramphenicol O-Acetyltransferase / genetics
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Chloramphenicol O-Acetyltransferase / metabolism
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Gene Expression
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Glutathione Transferase / genetics
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Glutathione Transferase / metabolism
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HIV / genetics
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HIV Long Terminal Repeat
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Humans
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NF-kappa B / antagonists & inhibitors
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NF-kappa B / metabolism*
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Proto-Oncogene Proteins / genetics
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Proto-Oncogene Proteins / metabolism*
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Recombinant Fusion Proteins / metabolism
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Repetitive Sequences, Nucleic Acid
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T-Lymphocytes / metabolism
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Transcription Factors
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Transcription, Genetic
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Transcriptional Activation
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Transfection
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Tumor Necrosis Factor-alpha / pharmacology
Substances
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Ankyrins
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B-Cell Lymphoma 3 Protein
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BCL3 protein, human
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NF-kappa B
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Proto-Oncogene Proteins
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Recombinant Fusion Proteins
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Transcription Factors
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Tumor Necrosis Factor-alpha
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Chloramphenicol O-Acetyltransferase
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Glutathione Transferase