Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1997-2-3
pubmed:abstractText
The transcription initiation factor TFIID is a multimeric protein complex composed of TATA box-binding protein (TBP) and many TBP-associated factors (TAF(II)s). TAF(II)s are important cofactors that mediate activated transcription by providing interaction sites for distinct activators. Here, we present evidence that human TAF(II)250 and its homologs in Drosophila and yeast have histone acetyltransferase (HAT) activity in vitro. HAT activity maps to the central, most conserved portion of dTAF(II)230 and yTAF(II)130. The HAT activity of dTAF(II)230 resembles that of yeast and human GCN5 in that it is specific for histones H3 and H4 in vitro. Our findings suggest that targeted histone acetylation at specific promoters by TAF(II)250 may be involved in mechanisms by which TFIID gains access to transcriptionally repressed chromatin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GCN5 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIID, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1261-70
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8980232-Acetyltransferases, pubmed-meshheading:8980232-Amino Acid Sequence, pubmed-meshheading:8980232-Animals, pubmed-meshheading:8980232-Chickens, pubmed-meshheading:8980232-DNA-Binding Proteins, pubmed-meshheading:8980232-Drosophila melanogaster, pubmed-meshheading:8980232-Fungal Proteins, pubmed-meshheading:8980232-Gene Expression Regulation, pubmed-meshheading:8980232-HeLa Cells, pubmed-meshheading:8980232-Histone Acetyltransferases, pubmed-meshheading:8980232-Humans, pubmed-meshheading:8980232-Insect Proteins, pubmed-meshheading:8980232-Macromolecular Substances, pubmed-meshheading:8980232-Molecular Sequence Data, pubmed-meshheading:8980232-Nuclear Proteins, pubmed-meshheading:8980232-Peptides, pubmed-meshheading:8980232-Protein Kinases, pubmed-meshheading:8980232-Recombinant Proteins, pubmed-meshheading:8980232-Saccharomyces cerevisiae, pubmed-meshheading:8980232-Saccharomyces cerevisiae Proteins, pubmed-meshheading:8980232-Sequence Deletion, pubmed-meshheading:8980232-Structure-Activity Relationship, pubmed-meshheading:8980232-Substrate Specificity, pubmed-meshheading:8980232-Transcription, Genetic, pubmed-meshheading:8980232-Transcription Factor TFIID, pubmed-meshheading:8980232-Transcription Factors
pubmed:year
1996
pubmed:articleTitle
The TAF(II)250 subunit of TFIID has histone acetyltransferase activity.
pubmed:affiliation
Department of Biology, University of Rochester, New York 14627, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't