| Literature DB >> 11163245 |
S B Seo1, P McNamara, S Heo, A Turner, W S Lane, D Chakravarti.
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.Entities:
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Year: 2001 PMID： 11163245 DOI： 10.1016/s0092-8674(01)00196-9
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582