JBC Transcription and Nuclear Factor Monoclonals

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Originally published In Press as doi:10.1074/jbc.M003815200 on August 15, 2000

J. Biol. Chem., Vol. 275, Issue 44, 34359-34364, November 3, 2000
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CREB-binding Protein/p300 Activates MyoD by Acetylation*

Anna PolesskayaDagger §, Arnaud DuquetDagger , Irina NaguibnevaDagger , Christoph Weise, Arlette Vervisch||, Eyal Bengal**, Ferdinand Hucho, Philippe RobinDagger , and Annick Harel-BellanDagger Dagger Dagger

From the Dagger  Laboratoire "Oncogenèse, Différenciation et Transduction du Signal," CNRS UPR 9079, Institut Fédératif André Lwoff, 7 rue Guy Moquet, Villejuif, France,  Institut für Chemie-Biochemie, Freie Universität, Thielallee 63, D-14 195 Berlin, || Service Commun de Cytofluorométrie, Institut Fédératif André Lwoff, 7 rue Guy Moquet, Villejuif, France, and ** Department of Biochemistry, Technion-Israel Institute of Technology, Haïfa 31096 Israel

The myogenic protein MyoD requires two nuclear histone acetyltransferases, CREB-binding protein (CBP)/p300 and PCAF, to transactivate muscle promoters. MyoD is acetylated by PCAF in vitro, which seems to increase its affinity for DNA. We here show that MyoD is constitutively acetylated in muscle cells. In vitro, MyoD is acetylated both by CBP/p300 and by PCAF on two lysines located at the boundary of the DNA binding domain. MyoD acetylation by CBP/p300 (as well as by PCAF) increases its activity on a muscle-specific promoter, as assessed by microinjection experiments. MyoD mutants that cannot be acetylated in vitro are not activated in the functional assay. Our results provide direct evidence that MyoD acetylation functionally activates the protein and show that both PCAF and CBP/p300 are candidate enzymes for MyoD acetylation in vivo.

* This work was supported by a grant from the Association Française contre les Myopathies and from the Association pour la Recherche sur le Cancer (to A. H-B.), a grant from the Fonds der Chemischen Industrie (to C. W. and F. H.), and European 5th Programme Cadre de Recherche et Développement Technologique Grant QLRT 1999-00866 (to A. H-B. and C. W.).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.

§ Recipient of a fellowship from the Federation of European Biochemical Societies.

Dagger Dagger To whom correspondence should be addressed. Tel.: 33-1-49-58-33-85; Fax: 33-1-49-58-33-07; E-mail: ahbellan@vjf.cnrs.fr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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