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Molecular and Cellular Biology, February 2000, p. 1299-1310, Vol. 20, No. 4
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The N-Terminal Domain of p73 Interacts with the CH1 Domain of p300/CREB Binding Protein and Mediates Transcriptional Activation and Apoptosis

Xiaoya Zeng,1 Xiaorong Li,1 Ashley Miller,1 Zhimin Yuan,2 Wuchao Yuan,3 Roland P. S. Kwok,3 Richard Goodman,3 and Hua Lu1,*

Department of Biochemistry and Molecular Biology1 and Vollum Institute,3 Oregon Health Sciences University, Portland, Oregon 97201, and Laboratory of Radiobiology, Harvard University School of Public Health, Boston, Massachusetts 021152

Received 1 October 1999/Returned for modification 9 November 1999/Accepted 15 November 1999

The newly identified p53 homolog p73 mimics the transcriptional function of p53. We have investigated the regulation of p73's transcriptional activity by p300/CREB binding protein (CBP). p73-p300 complexes were identified in HeLa cell extracts by cofractionation and coimmunoprecipitation assays. The p73-p300 interaction was confirmed in vitro by glutathione S-transferase-protein association assays and in vivo by coimmunoprecipitating the overexpressed p300 and p73 in human p53-free small-cell lung carcinoma H1299 or osteosarcoma Saos-2 cells. The N terminus but not the N-terminal truncation of p73 bound to the CH1 domain (amino acids [aa] 350 to 450) of p300/CBP. Accordingly, this p73 N-terminal deletion was unable to activate transcription or to induce apoptosis. Overexpression of either p300 or CBP stimulated transcription mediated by p73 but not its N-terminally deleted mutant in vivo. The N-terminal fragment from aa 19 to 597, but not the truncated fragment from aa 242 to 1700 of p300, reduced p73-mediated transcription markedly. p73-dependent transcription or apoptosis was partially impaired in either p300- or CBP-deficient human breast carcinoma MCF-7 or H1299 cells, suggesting that both coactivators mediate transcription by p73 in cells. These results demonstrate that the N terminus of p73 directly interacts with the N-terminal CH1 domain of p300/CBP to activate transcription.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, 3181 SW Sam Jackson Park Rd., Portland, OR 97201. Phone: (503) 494-7414. Fax: (503) 494-8393. E-mail: LUH{at}OHSU.edu.

Molecular and Cellular Biology, February 2000, p. 1299-1310, Vol. 20, No. 4
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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