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Molecular and Cellular Biology, January 2001, p. 476-487, Vol. 21, No. 2
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.2.476-487.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Stimulation of CREB Binding Protein Nucleosomal Histone Acetyltransferase Activity by a Class of Transcriptional Activators

Chi-Ju Chen,1 Zhong Deng,1 Alex Y. Kim,2 Gerd A. Blobel,2 and Paul M. Lieberman1,*

The Wistar Institute1 and Division of Hematology, The Children's Hospital of Philadelphia and the University of Pennsylvania School of Medicine,2 Philadelphia, Pennsylvania 19104

Received 31 March 2000/Returned for modification 15 September 2000/Accepted 27 October 2000

The transcriptional coactivator CREB binding protein (CBP) possesses intrinsic histone acetyltransferase (HAT) activity that is important for gene regulation. CBP binds to and cooperates with numerous nuclear factors to stimulate transcription, but it is unclear if these factors modulate CBP HAT activity. Our previous work showed that CBP interacts with the Epstein-Barr virus-encoded basic region zipper (b-zip) protein, Zta, and augments its transcriptional activity. Here we report that Zta strongly enhances CBP-mediated acetylation of nucleosomal histones. Zta stimulated the HAT activity of CBP that had been partially purified or immunoprecipitated from mammalian cells as well as from affinity-purified, baculovirus expressed CBP. Stimulation of nucleosome acetylation required the CBP HAT domain, the Zta DNA binding and transcription activation domain, and nucleosomal DNA. In addition to Zta, we found that two other b-zip proteins, NF-E2 and C/EBPalpha , strongly stimulated nucleosomal HAT activity. In contrast, several CBP-binding proteins, including phospho-CREB, JUN/FOS, GATA-1, Pit-1, and EKLF, failed to stimulate HAT activity. These results demonstrate that a subset of transcriptional activators enhance the nucleosome-directed HAT activity of CBP and suggest that nuclear factors may regulate transcription by altering substrate recognition and/or the enzymatic activity of chromatin modifying coactivators.

* Corresponding author. Mailing address: The Wistar Institute, 3601 Spruce St., Philadelphia, PA 19104-4268. Phone: (215) 898-9491. Fax: (215) 898-0663. E-mail: lieberman{at}wista.wistar.upenn.edu.

Molecular and Cellular Biology, January 2001, p. 476-487, Vol. 21, No. 2
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.2.476-487.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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