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Originally published In Press as doi:10.1074/jbc.C000722200 on November 13, 2000

J. Biol. Chem., Vol. 276, Issue 1, 48-52, January 5, 2001
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p300 Does Not Require Its Acetylase Activity to Stimulate p73 Function*

Xiaoya Zeng, Hunjoo Lee, Qinghong ZhangDagger , and Hua Lu§

From the Department of Biochemistry and Molecular Biology and the Dagger  Vollum Institute, Oregon Health Science University, Portland, Oregon 97201

We previously reported that p73, like p53, utilizes p300 or cAMP-response element-binding protein-binding protein as its coactivator. Here, we extended this work by further examining whether the intrinsic acetylase activity of p300 is necessary for stimulating p73 function. Although p300 acetylated the C-terminal fragment of p73 (amino acids 311-636) in vitro, it was unable to efficiently acetylate the full-length p73. Consistently, p300 did not acetylate p73 in vivo when both the proteins were overexpressed in cells. Also, an acetylase-defective mutant p300 named p300AT2 was able to elevate p73-dependent transcription in cells. p300 associated with p73 when forming DNA-protein complexes and stabilized p73 proteins. These results demonstrate that p300 does not need its acetylase activity to be a coactivator of p73.

* This work was supported by National Institutes of Health and American Cancer Society grants (to H. L.).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.

§ To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Oregon Health Science University, 3181 SW Sam Jackson Park Rd., Portland, OR 97201. Tel.: 503-494-7414; Fax: 503-494-8393; E-mail: LUH@OHSU.edu.

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