Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex

Sang beom Seo, Todd Macfarlan, Peter McNamara, Rui Hong, Yuki Mukai, Soyoung Heo, Debabrata Chakravarti*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

121 Scopus citations


Histone acetylation by p300/CBP and PCAF coactivators is considered to be a key mechanism of chromatin modification and transcriptional regulation. A multiprotein cellular complex, INHAT (inhibitor of acetyltransferases), containing the Set/TAF-Iβ oncoprotein and pp32 strongly inhibits the HAT activity of p300/CBP and PCAF by histone masking. Here we report that the INHAT complex and its subunits have overlapping but distinct HAT inhibitory and histone binding characteristics. We provide evidence suggesting that the histone binding and INHAT activity of pp32 can be regulated by its physical association with other INHAT subunits. In vivo colocalization and transfection studies show that pp32 INHAT domains are responsible for histone binding, HAT inhibitory activity, and repression of transcription. We propose that INHAT and its subunits may function by modulating histone acetyltransferases through a histone-masking mechanism and may play important regulatory roles in the establishment and maintenance of the newly proposed "histone code" of chromatin.

Original languageEnglish (US)
Pages (from-to)14005-14010
Number of pages6
JournalJournal of Biological Chemistry
Issue number16
StatePublished - Apr 19 2002

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry
  • Cell Biology


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