Abstract
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.
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Dates
Type | When |
---|---|
Created | 18 years, 2 months ago (June 5, 2007, 5:15 p.m.) |
Deposited | 3 years, 9 months ago (Nov. 13, 2021, 11:20 p.m.) |
Indexed | 3 months, 1 week ago (May 18, 2025, 12:03 p.m.) |
Issued | 34 years ago (Aug. 1, 1991) |
Published | 34 years ago (Aug. 1, 1991) |
Published Online | 34 years ago (Aug. 1, 1991) |
Published Print | 34 years ago (Aug. 1, 1991) |
@article{Kerr_1991, title={The rel-associated pp40 protein prevents DNA binding of Rel and NF-kappa B: relationship with I kappa B beta and regulation by phosphorylation.}, volume={5}, ISSN={1549-5477}, url={http://dx.doi.org/10.1101/gad.5.8.1464}, DOI={10.1101/gad.5.8.1464}, number={8}, journal={Genes & Development}, publisher={Cold Spring Harbor Laboratory}, author={Kerr, L D and Inoue, J and Davis, N and Link, E and Baeuerle, P A and Bose, H R and Verma, I M}, year={1991}, month=aug, pages={1464–1476} }