Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein.

Acetylation of histones by p300/CBP and PCAF is considered to be a critical step in transcriptional regulation. In order to understand the role of cellular activities that modulate histone acetylation and transcription, we have purified and characterized a multiprotein cellular complex that potently inhibits the histone acetyltransferase activity of p300/CBP ...
and PCAF. We have mapped a novel acetyltransferase-inhibitory domain of this INHAT (inhibitor of acetyltransferases) complex that binds to histones and masks them from being acetyltransferase substrates. Endogenous INHAT subunits, which include the Set/TAF-Ibeta oncoprotein, associate with chromatin in vivo and can block coactivatormediated transcription when transfected in cells. We propose that histone masking by INHAT plays a regulatory role in chromatin modification and serves as a novel mechanism of transcriptional regulation.
Mesh Terms:
Acetylation, Acetyltransferases, Cell Cycle Proteins, Chromatin, Chromosomal Proteins, Non-Histone, Chromosome Mapping, Hela Cells, Histone Acetyltransferases, Histone Chaperones, Histones, Humans, Nuclear Proteins, Phosphoproteins, Protein Binding, Protein Structure, Tertiary, Proteins, Receptors, Retinoic Acid, Saccharomyces cerevisiae Proteins, Signal Transduction, Transcription Factors, Transcription, Genetic, p300-CBP Transcription Factors
Cell
Date: Jan. 12, 2001
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