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Molecular and Cellular Biology, January 2000, p. 556-562, Vol. 20, No. 2
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.
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

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