The Rel-associated pp40 protein prevents DNA binding of Rel and NF-κB : relationship with IκBβ and regulation by phosphorylation

The product of proto-oncogene Rel associates with a number of cellular proteins. We have studied the effect of one of them, a phosphoprotein of 40 kD (pp40), on the DNA-binding activity of the Rel protein. We demonstrate that purified pp40 not only inhibits the binding of Rel, but also NF-kappa B (p...

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Bibliographic Details
Published in:Genes & development 1991-08, Vol.5 (8), p.1464-1476
Main Authors: KERR, L. D, INOUE, J, DAVIS, N, LINK, E, BAEUERLE, P. A, BOSE, H. R, VERMA, I. M
Format: Article
Language:English
Subjects:
Animals
Base Sequence
Binding Sites
Biological and medical sciences
Cell Line
Cell Transformation, Neoplastic
DNA-Binding Proteins - metabolism
Enhancer Elements, Genetic
Fundamental and applied biological sciences. Psychology
Homeostasis
Immunoglobulin kappa-Chains - genetics
Mice
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
NF-kappa B - metabolism
Oligonucleotide Probes
Peptide Fragments - isolation & purification
Phosphoproteins - metabolism
Phosphorylation
Protein Kinase C - metabolism
Protein Kinases - metabolism
Protein-Tyrosine Kinases - metabolism
Proto-Oncogene Proteins - metabolism
Proto-Oncogene Proteins c-rel
Proto-Oncogenes
Repressor Proteins - metabolism
Transcription. Transcription factor. Splicing. Rna processing
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Summary:The product of proto-oncogene Rel associates with a number of cellular proteins. We have studied the effect of one of them, a phosphoprotein of 40 kD (pp40), on the DNA-binding activity of the Rel protein. We demonstrate that purified pp40 not only inhibits the binding of Rel, but also NF-kappa B (p50-p65) heterocomplex to DNA. Additionally, I kappa B beta, but not I kappa B alpha, also prevented the binding of Rel to the kappa B site. I kappa B beta and pp40 are related proteins because (1) they share a number of common tryptic peptides, (2) their inhibitory effect on DNA binding can be abolished by preincubation with pp40-specific antiserum, and (3) labeled I kappa B beta can be immunoprecipitated with pp40 antibodies. pp40 is part of the Rel complex present in the cytoplasm and nuclear extracts of WEHI-231 cells. The activity of pp40 to inhibit the DNA binding of Rel and NF-kappa B is modulated by phosphorylation.
ISSN:0890-9369
1549-5477
DOI:10.1101/gad.5.8.1464