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Adenoviral ElA-associated protein p300 as a functional homologue of the transcriptional co-activator CBP

Nature volume 374, pages 85–88 (1995)Cite this article

Abstract

THE 265K nuclear protein CBP was initially identified as a co-activator for the protein kinase A (PKA)-phosphorylated form of the transcription factor CREB1. The domains in CBP that are involved in CREB binding and transcriptional activation are highly related to the adenoviral ElA-associated cellular protein p300 (refs 2, 3), and to two hypothetical proteins from Caenorhabditis elegans, R10E11.1 and K03H1.10 (refs 4 and 5, respectively), whose functions are unknown. Here, we show that CBP and p300 have similar binding affinity for the PKA-phosphorylated form of CREB, and that p300 can substitute for CBP in potentiating CREB-activated gene expression. We find that E1A binds to CBP through a domain conserved with p300 and represses the CREB-dependent co-activator functions of both CBP and p300. Our results indicate that the gene repression and cell immortalization functions associated with El A involve the inactivation of a family of related proteins that normally participate in second-messenger-regulated gene expression.

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Author notes

  1. Marian L. Harter: Department of Molecular Biology, Cleveland Clinic Research Institute, Cleveland, Ohio 44195, USA

  2. Richard H. Goodman: To whom correspondence should be addressed

Authors and Affiliations

  1. Vollum Institute, Oregon Health Sciences University, 3181 SW Sam Jackson Park Road, Portland, Oregon, 97201, USA

    James R. Lundblad, Roland P. S. Kwok, Megan E. Laurance, Marian L. Harter & Richard H. Goodman

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  1. James R. Lundblad
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  2. Roland P. S. Kwok
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  3. Megan E. Laurance
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  4. Marian L. Harter
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  5. Richard H. Goodman
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Lundblad, J., Kwok, R., Laurance, M. et al. Adenoviral ElA-associated protein p300 as a functional homologue of the transcriptional co-activator CBP. Nature 374, 85–88 (1995). https://doi.org/10.1038/374085a0

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