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

Sang beom Seo, Peter McNamara, Soyoung Heo, April Turner, William S. Lane, Debabrata Chakravarti*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

366 Scopus citations

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-Iβ 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.

Original languageEnglish (US)
Pages (from-to)119-130
Number of pages12
JournalCell
Volume104
Issue number1
DOIs
StatePublished - Jan 12 2001

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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