Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-12-1
pubmed:abstractText
The transcriptional coactivators CBP and P/CAF are required for activation of transcription from the IFN beta enhanceosome. We show that CBP and P/CAF acetylate HMG I(Y), the essential architectural component required for enhanceosome assembly, at distinct lysine residues, causing distinct effects on transcription. Thus, in the context of the enhanceosome, acetylation of HMG I by CBP, but not by P/CAF, leads to enhanceosome destabilization and disassembly. We demonstrate that acetylation of HMG I(Y) by CBP is essential for turning off IFN beta gene expression. Finally, we show that the acetyltransferase activities of CBP and P/CAF modulate both the strength of the transcriptional response and the kinetics of virus-dependent activation of the IFN beta gene.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/CREB-Binding Protein, http://linkedlifedata.com/resource/pubmed/chemical/Chromatin Assembly Factor-1, http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HMGA1a Protein, http://linkedlifedata.com/resource/pubmed/chemical/High Mobility Group Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Interferon-beta, http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
457-67
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9809067-Acetylation, pubmed-meshheading:9809067-Animals, pubmed-meshheading:9809067-Binding Sites, pubmed-meshheading:9809067-COS Cells, pubmed-meshheading:9809067-CREB-Binding Protein, pubmed-meshheading:9809067-Chromatin Assembly Factor-1, pubmed-meshheading:9809067-Chromosomal Proteins, Non-Histone, pubmed-meshheading:9809067-DNA-Binding Proteins, pubmed-meshheading:9809067-Drosophila, pubmed-meshheading:9809067-Enhancer Elements, Genetic, pubmed-meshheading:9809067-Gene Expression Regulation, Neoplastic, pubmed-meshheading:9809067-HMGA1a Protein, pubmed-meshheading:9809067-High Mobility Group Proteins, pubmed-meshheading:9809067-Interferon-beta, pubmed-meshheading:9809067-Mutagenesis, pubmed-meshheading:9809067-NF-kappa B, pubmed-meshheading:9809067-Neoplasm Proteins, pubmed-meshheading:9809067-Nuclear Proteins, pubmed-meshheading:9809067-Protein Structure, Tertiary, pubmed-meshheading:9809067-Trans-Activators, pubmed-meshheading:9809067-Transcription Factors
pubmed:year
1998
pubmed:articleTitle
Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome.
pubmed:affiliation
Department of Biochemistry, and Molecular Biophysics, Columbia University, New York, New York 10032, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't