Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein.
basic_science · Level V
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Abstract
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.
Medical subject headings
- Acetyltransferases
- Cell Cycle Proteins
- Chromosomal Proteins, Non-Histone
- Histones
- Saccharomyces cerevisiae Proteins
- Transcription Factors