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B RelA via the Transcriptional Integrator p3001
Johns Hopkins Oncology Center, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21287-8967 [R. R., B. M., Y. v. H., G. C. B., E. J. F., A. B.]; Sbarro Institute for Cancer Research and Molecular Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107 [A. G.]; and Howard Hughes Medical Institute, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104 [W. S. E-D.]
The p53 tumor suppressor gene plays an instrumental role in transcriptional regulation of target genes involved in cellular stress responses. p53-dependent transactivation and transrepression require its interaction with p300/CBP, a coactivator that also interacts with the RelA subunit of nuclear factor-
B. We find that p53 inhibits RelA-dependent transactivation without altering RelA expression or inducible B-DNA binding. p53-mediated repression of RelA is relieved by p300 overexpression and the increased RelA activity conferred by p53-deficiency is counteracted by either transactivation domain-deficient p300 fragments that bind RelA or a transdominant mutant of IB
. Our results suggest that p53 can regulate diverse B-dependent cellular responses.
1 Funded by Grant 1 R29CA71660-01A1 from the National Cancer Institute and Grant R21 CA/ES66204 from the NIH (to A. B.). A. B. is a recipient of a Passano Physician Scientist award, a Valvano Foundation Scholar award, a Jose Carreras American Society of Hematology Scholar award, and grants from the American Cancer Society.
2 These authors contributed equally to this work.
3 To whom requests for reprints should be addressed, at 3-120 Johns Hopkins Oncology Center, 600 North Wolfe Street, Baltimore, MD 21287-8967. Phone: (410) 614-3844; Fax: (410) 955-1969; E-mail: rbedi@welchlink.welch.jhu.edu.
Received 7/29/98. Accepted 8/31/98.
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