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Molecular and Cellular Biology, January 2000, p. 556-562, Vol. 20, No. 2
0270-7306/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Essential Cofactor TRRAP Recruits the Histone Acetyltransferase hGCN5 to c-Myc

Steven B. McMahon,dagger Marcelo A. Wood, and Michael D. Cole*

Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014

Received 22 June 1999/Returned for modification 28 July 1999/Accepted 22 October 1999

The c-Myc protein functions as a transcription factor to facilitate oncogenic transformation; however, the biochemical and genetic pathways leading to transformation remain undefined. We demonstrate here that the recently described c-Myc cofactor TRRAP recruits histone acetylase activity, which is catalyzed by the human GCN5 protein. Since c-Myc function is inhibited by recruitment of histone deacetylase activity through Mad family proteins, these opposing biochemical activities are likely to be responsible for the antagonistic biological effects of c-Myc and Mad on target genes and ultimately on cellular transformation.

* Corresponding author. Mailing address: Department of Molecular Biology, Princeton University, Princeton, NJ 08544-1014. Phone: (609) 258-5936. Fax: (609) 258-2759. E-mail: mcole{at}molbio.princeton.edu.

dagger Present address: The Wistar Institute, Philadelphia, PA 19104-4268.

Molecular and Cellular Biology, January 2000, p. 556-562, Vol. 20, No. 2
0270-7306/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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