Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A.
Histone acetyltransferases (HAT) play a critical role in transcriptional control by relieving repressive effects of chromatin, and yet how HATs themselves are regulated remains largely unknown. Here, it is shown that Twist directly binds two independent HAT domains of acetyltransferases, p300 and p300/CBP-associated factor (PCAF), and directly regulates their HAT ... activities. The N terminus of Twist is a primary domain interacting with both acetyltransferases, and the same domain is required for inhibition of p300-dependent transcription by Twist. Adenovirus E1A protein mimics the effects of Twist by inhibiting the HAT activities of p300 and PCAF. These findings establish a cogent argument for considering the HAT domains as a direct target for acetyltransferase regulation by both a cellular transcription factor and a viral oncoprotein.
Mesh Terms:
Acetyltransferases, Adenovirus E1A Proteins, Animals, COS Cells, Cells, Cultured, E1A-Associated p300 Protein, Enzyme Activation, Histone Acetyltransferases, Mice, Nuclear Proteins, Oncogene Proteins, Viral, Peptide Fragments, Saccharomyces cerevisiae Proteins, Trans-Activators, Transcription Factors, Transcription, Genetic, Twist Transcription Factor
Acetyltransferases, Adenovirus E1A Proteins, Animals, COS Cells, Cells, Cultured, E1A-Associated p300 Protein, Enzyme Activation, Histone Acetyltransferases, Mice, Nuclear Proteins, Oncogene Proteins, Viral, Peptide Fragments, Saccharomyces cerevisiae Proteins, Trans-Activators, Transcription Factors, Transcription, Genetic, Twist Transcription Factor
Cell
Date: Feb. 05, 1999
PubMed ID: 10025406
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