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

doi:10.1128/MCB.21.16.5312-5320.2001

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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 transcriptionand that modifies transcription factor affinity for binding siteson DNA, stability, and/or nuclear localization. Here, we presentboth in vitro and in vivo evidence that acetylation increasesthe affinity of myogenic factor MyoD for acetyltransferases CBPand p300. In myogenic cells, the fraction of endogenous MyoD thatis acetylated was found associated with CBP or p300. In vitro,the interaction between MyoD and CBP was more resistant to highsalt concentrations and was detected with lower doses of MyoDwhen MyoD was acetylated. Interestingly, an analysis of CBP mutantsrevealed that the interaction with acetylated MyoD involves thebromodomain of CBP. In live cells, MyoD mutants that cannot beacetylated did not associate with CBP or p300 and were stronglyimpaired in their ability to cooperate with CBP for transcriptionalactivation of a muscle creatine kinase-luciferase construct. Takentogether, our data suggest a new mechanism for activation of proteinfunction by acetylation and demonstrate for the first time anacetylation-dependent interaction between the bromodomain of CBPand a nonhistoneprotein.

^* 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.

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