Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2007-1-22
pubmed:abstractText
Brd2 is a novel protein kinase and plays a role in cell cycle-responsive transcription. Recent studies show that Brd2 contributes to E2F-1 regulated cell cycle progression. In this process, Brd2 exhibits scaffold or transcriptional adapter functions and mediates recruitment of both E2F-1 transcription factors and chromatin-remodelling activity to the E2F-1-resposive promoter. In the present study, we show that Brd2 is also a TBP-associated protein and a 26 amino acids peptide in the first bromodomain of Brd2 is essential for Brd2-TBP interaction. We found that serum stimulation of serum starved NIH/3T3 cells efficiently induces the formation of the Brd2-E2F-1-TBP complex in vivo. In this process, Brd2 plays a pivotal role in the recruitment of TBP into a E2F-1 transcriptional complex, as tested in overexpression assay and at the endogenous level. Furthermore, the 26 amino acid peptide that mediates Brd2-TBP interaction is proved to be critical for Brd2-dependent transactivation on E2F-1-responsive promoters, and moreover, Brd2 and E2F-1 may cooperatively participate in various serum-induced transactivation processes in Luciferase-reporter assays. Thus taken together, because Brd2 may recruit a HAT in its transactivational complex and E2F-1 has been found to stimulate transcription by recruiting acetyltransferase and cofactors GCN5, we predict that Brd2 and E2F-1 may act in a cooperative way to introduce an optimal environment for TBP binding to the TATA-element of gene promoters.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:volume
294
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
45-54
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Brd2 is a TBP-associated protein and recruits TBP into E2F-1 transcriptional complex in response to serum stimulation.
pubmed:affiliation
National Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, Hubei, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't