Abstract
We show that the product of the protooncogene c-rel is a constituent of an NF-kappa B-like complex that binds to the kappa B site originally identified in the enhancer of immunoglobulin kappa light chain gene. c-rel protein synthesized in bacteria binds to the kappa B site in a sequence-specific manner. The rel-kappa B complex can be disrupted by incubation with anti-rel antibodies. The rel protein can form oligomers. The c-rel protein can activate transcription from promoters containing kappa B sites; v-rel, on the other hand, suppresses the transcription of genes linked to kappa B sites. Thus, v-rel may interfere with the normal transcriptional machinery of the cell by acting as a dominant negative mutant.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Binding Sites
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Gene Expression Regulation*
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In Vitro Techniques
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Mice
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Molecular Sequence Data
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NF-kappa B / physiology*
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Oncogene Proteins v-rel
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Proto-Oncogene Proteins / physiology*
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Proto-Oncogene Proteins c-rel
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Recombinant Proteins
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Regulatory Sequences, Nucleic Acid
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Repressor Proteins / physiology
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Retroviridae Proteins, Oncogenic / physiology*
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Transcription Factors / physiology
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Transcription, Genetic
Substances
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NF-kappa B
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Oncogene Proteins v-rel
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Proto-Oncogene Proteins
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Proto-Oncogene Proteins c-rel
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Recombinant Proteins
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Repressor Proteins
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Retroviridae Proteins, Oncogenic
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Transcription Factors