TY - JOUR
T1 - A viral mechanism for inhibition of P300 and PCAF acetyltransferase activity
AU - Chakravarti, Debabrata
AU - Ogryzko, Vasily
AU - Kao, Hung Ying
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.
AB - 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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U2 - 10.1016/S0092-8674(00)80552-8
DO - 10.1016/S0092-8674(00)80552-8
M3 - Article
C2 - 10025405
AN - SCOPUS:0033524942
VL - 96
SP - 393
EP - 403
JO - Cell
JF - Cell
SN - 0092-8674
IS - 3
ER -