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

doi:10.1016/S0092-8674(00)80552-8

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

^*Corresponding author for this work

Obstetrics and Gynecology

Research output: Contribution to journal › Article › peer-review

289 Scopus citations

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 language	English (US)
Pages (from-to)	393-403
Number of pages	11
Journal	Cell
Volume	96
Issue number	3
DOIs	https://doi.org/10.1016/S0092-8674(00)80552-8
State	Published - Feb 5 1999

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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title = "A viral mechanism for inhibition of P300 and PCAF acetyltransferase activity",

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.",

author = "Debabrata Chakravarti and Vasily Ogryzko and Kao, {Hung Ying} and Alyssa Nash and Hongwu Chen and Yoshihiro Nakatani and Evans, {Ronald M.}",

note = "Funding Information: We thank Drs. Ira Schulman and Richard Lin for critically reading the manuscript. We acknowledge Damien Wilpitz and Ester Banayo for technical assistance. D. C. is supported by funding through the University of Pennsylvania Cancer Center{\textquoteright}s American Cancer Society Institutional Research Grant and Pilot Projects Program. H.-Y. K. is a postdoctoral fellow of Leukemia Society of America. R. M. E. is an investigator of the Howard Hughes Medical Institute at the Salk Institute and March of Dimes Chair in Molecular Developmental Biology. We thank the Joe W. and Dorothy Dorsett Brown Foundation and the Drown Foundation for their financial support. ",

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AU - Chakravarti, Debabrata

AU - Ogryzko, Vasily

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AU - Nash, Alyssa

AU - Chen, Hongwu

AU - Nakatani, Yoshihiro

AU - Evans, Ronald M.

N1 - Funding Information: We thank Drs. Ira Schulman and Richard Lin for critically reading the manuscript. We acknowledge Damien Wilpitz and Ester Banayo for technical assistance. D. C. is supported by funding through the University of Pennsylvania Cancer Center’s American Cancer Society Institutional Research Grant and Pilot Projects Program. H.-Y. K. is a postdoctoral fellow of Leukemia Society of America. R. M. E. is an investigator of the Howard Hughes Medical Institute at the Salk Institute and March of Dimes Chair in Molecular Developmental Biology. We thank the Joe W. and Dorothy Dorsett Brown Foundation and the Drown Foundation for their financial support.

PY - 1999/2/5

Y1 - 1999/2/5

N2 - 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.

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