A viral mechanism for inhibition of P300 and PCAF acetyltransferase activity

Debabrata Chakravarti, Vasily Ogryzko, Hung Ying Kao, Alyssa Nash, Hongwu Chen, Yoshihiro Nakatani, Ronald M. Evans

Research output: Contribution to journalArticlepeer-review

289 Citations (Scopus)

Abstract

Nucleosomal histone modification is believed to be a critical step in the activation of RNA polymerase II-dependent transcription. p300/CBP and PCAF histone acetyltransferases (HATs) are coactivators for several transcription factors, including nuclear hormone receptors, p53, and Stat1α, and participate in transcription by forming an activation complex and by promoting histone acetylation. The adenoviral E1A oncoprotein represses transcriptional signaling by binding to p300/CBP and displacing PCAF and p/CIP proteins from the complex. Here, we show that E1A directly represses the HAT activity of both p300/CBP and PCAF in vitro and p300-dependent transcription in vivo. Additionally, E1A inhibits nucleosomal histone modifications by the PCAF complex and blocks p53 acetylation. These results demonstrate the modulation of HAT activity as a novel mechanism of transcriptional regulation.

Original languageEnglish
Pages (from-to)393-403
Number of pages11
JournalCell
Volume96
Issue number3
DOIs
Publication statusPublished - 1999 Feb 5

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

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