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Originally published In Press as doi:10.1074/jbc.M008231200 on September 27, 2000

J. Biol. Chem., Vol. 276, Issue 2, 1510-1515, January 12, 2001
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p53 Amino Acids 339-346 Represent the Minimal p53 Repression Domain*

Tse-Ming HongDagger §, Jeremy J. W. Chen||, Konan Peck§, Pan-Chyr YangDagger §**Dagger Dagger , and Cheng-Wen WuDagger §§§

From the Dagger  Graduate Institute of Molecular Biology, College of Medicine, National Taiwan University, Taipei, Taiwan 100, Republic of China, § Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan 115, Republic of China, || Office for Clinical Research, National Taiwan University Hospital, ** Department of Internal Medicine, School of Medicine, National Taiwan University, Taipei, Taiwan 100, Republic of China, and the §§ National Health Research Institute, Taipei, Taiwan 115, Republic of China

The p53 tumor suppressor protein functions as an activator and also as a repressor of gene transcription. Currently, the mechanism of transcriptional repression by p53 remains poorly understood. To help clarify this mechanism, we carried out studies designed to identify the minimal repression domain that inhibits p53 transcriptional activities. We found only eight amino acids (339) of the COOH-terminal domain (termed P53MRD) that possess activities of repression. The exact location of this minimal domain is on the E6-binding region, and it lacks the ability of tetramerization. P53MRD is able to repress the transcription of p53 while not affecting VP16. The mutants (amino acids M340P and F341D) of native p53 also lost transcriptional repression of the thymidine kinase chloramphenicol acetyltransferase promoter. These results suggest that this eight-amino acid element is required for the repression of p53.

* This work was supported by grants from Academia Sinica.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Both authors contributed equally to this work.

Dagger Dagger To whom correspondence should be addressed: Dept. of Internal Medicine, National Taiwan University Hospital, 7, Chung-Shan South Road, Taipei 100, Taiwan. Tel.: 886-2-23562116; Fax: 886-2-23582867 or 886-2-23934176; E-mail: pcyang@ha.mc.ntu.edu.tw.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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