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Molecular and Cellular Biology, August 2001, p. 5312-5320, Vol. 21, No. 16
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.16.5312-5320.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Interaction between Acetylated MyoD and the Bromodomain of CBP and/or p300

Anna Polesskaya,1 Irina Naguibneva,1 Arnaud Duquet,1 Eyal Bengal,2 Philippe Robin,1 and Annick Harel-Bellan1,*

Laboratoire Oncogenèse, Différenciation et Transduction du Signal, CNRS UPR 9079, Institut André Lwoff, Villejuif, France,1 and Department of Biochemistry, Technion-Israel Institute of Technology, Haïfa 31096, Israel2

Received 13 December 2000/Returned for modification 22 January 2001/Accepted 7 May 2001

Acetylation is emerging as a posttranslational modification of nuclear proteins that is essential to the regulation of transcription and that modifies transcription factor affinity for binding sites on DNA, stability, and/or nuclear localization. Here, we present both in vitro and in vivo evidence that acetylation increases the affinity of myogenic factor MyoD for acetyltransferases CBP and p300. In myogenic cells, the fraction of endogenous MyoD that is acetylated was found associated with CBP or p300. In vitro, the interaction between MyoD and CBP was more resistant to high salt concentrations and was detected with lower doses of MyoD when MyoD was acetylated. Interestingly, an analysis of CBP mutants revealed that the interaction with acetylated MyoD involves the bromodomain of CBP. In live cells, MyoD mutants that cannot be acetylated did not associate with CBP or p300 and were strongly impaired in their ability to cooperate with CBP for transcriptional activation of a muscle creatine kinase-luciferase construct. Taken together, our data suggest a new mechanism for activation of protein function by acetylation and demonstrate for the first time an acetylation-dependent interaction between the bromodomain of CBP and a nonhistone protein.

* Corresponding author. Mailing address: Laboratoire Oncogenèse, Différenciation et Transduction du Signal, CNRS UPR 9079, Institut André Lwoff, 7 rue Guy Moquet, Villejuif, France. Phone: 33-(0)1-49 58 33 85. Fax: 33-(0)1-49 58 33 07. E-mail: ahbellan{at}vjf.cnrs.fr.

Molecular and Cellular Biology, August 2001, p. 5312-5320, Vol. 21, No. 16
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.16.5312-5320.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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