Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1995-6-23
pubmed:abstractText
YY1 represses transcription when bound upstream of transcriptional initiation sites. This repression can be relieved by adenovirus E1A. Here, we present genetic evidence that the ability of E1A to relieve YY1 repression was impaired by mutations that affect E1A binding to its associated protein p300. This suggests that E1A may modulate the repressor activity of YY1 by binding to p300, which may be physically complexed with YY1. A YY1/p300 protein complex in vivo was demonstrated by several independent approaches, and the YY1-interacting domain was mapped to the carboxy-terminal region of p300, distinct from the E1A-binding site. Unlike E2F/RB, the YY1/p300 complex is not disrupted by E1A. Functional studies using recombinant p300 demonstrated unequivocally that p300 is capable of mediating E1A-induced transcriptional activation through YY1. Taken together, these results reveal, for the first time, a YY1/p300 complex that is targeted by E1A and demonstrate a function for p300 in mediating interactions between YY1 and E1A. Our data thus identify YY1 as a partner protein for p300 and uncover a molecular mechanism for the relief of YY1-mediated repression by E1A.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenovirus E1A Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/E1A-Associated p300 Protein, http://linkedlifedata.com/resource/pubmed/chemical/Erythroid-Specific DNA-Binding..., http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/YY1 Transcription Factor, http://linkedlifedata.com/resource/pubmed/chemical/YY1 protein, human
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0890-9369
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1188-98
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:7758944-Adenoviridae Infections, pubmed-meshheading:7758944-Adenovirus E1A Proteins, pubmed-meshheading:7758944-Base Sequence, pubmed-meshheading:7758944-Binding Sites, pubmed-meshheading:7758944-DNA Primers, pubmed-meshheading:7758944-DNA-Binding Proteins, pubmed-meshheading:7758944-E1A-Associated p300 Protein, pubmed-meshheading:7758944-Erythroid-Specific DNA-Binding Factors, pubmed-meshheading:7758944-Gene Expression, pubmed-meshheading:7758944-Gene Expression Regulation, Viral, pubmed-meshheading:7758944-HeLa Cells, pubmed-meshheading:7758944-Humans, pubmed-meshheading:7758944-Molecular Sequence Data, pubmed-meshheading:7758944-Nuclear Proteins, pubmed-meshheading:7758944-Protein Binding, pubmed-meshheading:7758944-RNA, Messenger, pubmed-meshheading:7758944-Repressor Proteins, pubmed-meshheading:7758944-Structure-Activity Relationship, pubmed-meshheading:7758944-Trans-Activators, pubmed-meshheading:7758944-Transcription Factors, pubmed-meshheading:7758944-YY1 Transcription Factor
pubmed:year
1995
pubmed:articleTitle
Relief of YY1 transcriptional repression by adenovirus E1A is mediated by E1A-associated protein p300.
pubmed:affiliation
Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't