The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc.

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.
Mesh Terms:
Acetyltransferases, Adaptor Proteins, Signal Transducing, Animals, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, Basic-Leucine Zipper Transcription Factors, Carrier Proteins, Catalytic Domain, Cell Cycle Proteins, Cell Line, Cell Transformation, Neoplastic, DNA-Binding Proteins, Dimerization, Genes, Essential, Hela Cells, Histone Acetyltransferases, Histone Deacetylases, Humans, Models, Biological, Nuclear Proteins, Precipitin Tests, Protein Binding, Proto-Oncogene Proteins c-myc, Rats, Recombinant Fusion Proteins, Repressor Proteins, Saccharomyces cerevisiae Proteins, Trans-Activators, Transcription Factors, p300-CBP Transcription Factors
Mol. Cell. Biol.
Date: Jan. 01, 2000
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