期刊
CELL
卷 104, 期 1, 页码 119-130出版社
CELL PRESS
DOI: 10.1016/S0092-8674(01)00196-9
关键词
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资金
- NIDDK NIH HHS [R01-DK57079-01A1, P30-DK19925, R01 DK057079] Funding Source: Medline
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-I beta oncoprotein, associate with chromatin in vivo and can block coactivator-mediated 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.
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