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Molecular and Cellular Biology, June 1999, p. 4241-4246, Vol. 19, No. 6
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Specificity of Cyclin E-Cdk2, TFIIB, and E1A Interactions with a Common Domain of the p300 Coactivator

Lisa K. Felzien,dagger Susan Farrell, Jonathan C. Betts, Rashid Mosavin,Dagger and Gary J. Nabel*

Howard Hughes Medical Institute, University of Michigan Medical Center, Departments of Internal Medicine and Biological Chemistry, Ann Arbor, Michigan 48109-0650

Received 8 September 1998/Returned for modification 8 December 1998/Accepted 24 March 1999

The p300 and CREB binding protein (CBP) transcriptional coactivators interact with a variety of transcription factors and regulate their activity. Among the interactions that have been described, the COOH-terminal region of p300 binds to cyclin E-cyclin-dependent kinase 2 (cyclin E-Cdk2) and TFIIB, as well as to the E1A gene products of adenovirus. Inhibition of Cdk activity by Cdk inhibitors, such as p21 or p27, potentiates NF-kappa B activity and provides a mechanism to coordinate cell cycle progression with the transcription of genes expressed during growth arrest. In this report, we analyze the specific domains of p300 required for the binding of p300 to cyclin E-Cdk2, TFIIB, and E1A and the ability of these proteins to interact with p300, alone or in combination. 12S E1A, an inhibitor of p300-dependent transcription, reduces the binding of TFIIB, but not that of cyclin E-Cdk2, to p300. In contrast, 13S E1A, a pleiotropic transcriptional activator, does not inhibit TFIIB binding to p300, although it enhances the interaction of cyclin E-Cdk2 with p300. Modification of cyclin E-Cdk2 is most likely required for association with p300 since the interaction is observed only with cyclin E-Cdk2 purified from mammalian cells. Domain swap studies show that the cyclin homology domain of TFIIB is involved in interactions with p300, although the homologous region from cyclin E does not mediate this interaction. These findings suggest that p300 or CBP function is regulated by interactions of various proteins with a common coactivator domain.

* Corresponding author. Mailing address: Howard Hughes Medical Institute, University of Michigan Health Center, Departments of Internal Medicine and Biological Chemistry, 1150 W. Medical Center Dr., MSRB I, Ann Arbor, MI 48109-0650. Phone: (734) 647-4798. Fax: (734) 647-4730. E-mail: gnabel{at}umich.edu.

dagger Present address: University of Kansas Medical School, Department of Anatomy and Cell Biology, Kansas City, KS 66160.

Dagger Present address: Henry Ford Hospital, Department of Pharmacy Services, Detroit, MI 48202-2689.

Molecular and Cellular Biology, June 1999, p. 4241-4246, Vol. 19, No. 6
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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