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

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-Ibeta 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.

Pubmed ID: 11830591 RIS Download

Mesh terms: 3T3 Cells | Animals | Chromatin | Dose-Response Relationship, Drug | E1A-Associated p300 Protein | HeLa Cells | Histones | Humans | Mice | Microscopy, Fluorescence | Nuclear Proteins | Peptides | Phosphoproteins | Plasmids | Precipitin Tests | Protein Binding | Protein Structure, Tertiary | Recombinant Proteins | Trans-Activators | Transcription, Genetic | Transcriptional Activation | Transfection

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Associated grants

  • Agency: NIDDK NIH HHS, Id: R01 DK057079
  • Agency: NIDDK NIH HHS, Id: P30-DK50306
  • Agency: NIDDK NIH HHS, Id: R01-DK57079

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