rdf:type |
|
lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0035681,
umls-concept:C0040649,
umls-concept:C0220905,
umls-concept:C0449432,
umls-concept:C0663446,
umls-concept:C1179435,
umls-concept:C1422073,
umls-concept:C1446409,
umls-concept:C1511331,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1705248
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pubmed:issue |
4
|
pubmed:dateCreated |
2005-8-19
|
pubmed:abstractText |
Brd4 is a mammalian bromodomain protein that binds to acetylated chromatin. Proteomic analysis revealed that Brd4 interacts with cyclinT1 and Cdk9 that constitutes core positive transcription elongation factor b (P-TEFb). Brd4 interacted with P-TEFb in the living nucleus through its bromodomain. About half of P-TEFb was bound to the inhibitory subunit and functionally inactive. Brd4 interacted with P-TEFb that was free of the inhibitory subunit. An increase in Brd4 expression led to increased P-TEFb-dependent phosphorylation of RNA polymerase II (RNAPII) CTD and stimulation of transcription from promoters in vivo. Conversely, a reduction in Brd4 expression by siRNA reduced CTD phosphorylation and transcription, revealing that Brd4 is a positive regulatory component of P-TEFb. In chromatin immunoprecipitation (ChIP) assays, the recruitment of P-TEFb to a promoter was dependent on Brd4 and was enhanced by an increase in chromatin acetylation. Together, P-TEFb alternately interacts with Brd4 and the inhibitory subunit to maintain functional equilibrium in the cell.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Brd4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cdk9 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 9,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins, Fusion,
http://linkedlifedata.com/resource/pubmed/chemical/Positive Transcriptional...,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
|
pubmed:issn |
1097-2765
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
523-34
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16109376-Animals,
pubmed-meshheading:16109376-Cyclin-Dependent Kinase 9,
pubmed-meshheading:16109376-DNA, Complementary,
pubmed-meshheading:16109376-Mice,
pubmed-meshheading:16109376-Nuclear Proteins,
pubmed-meshheading:16109376-Oncogene Proteins, Fusion,
pubmed-meshheading:16109376-Positive Transcriptional Elongation Factor B,
pubmed-meshheading:16109376-Promoter Regions, Genetic,
pubmed-meshheading:16109376-RNA, Small Nuclear,
pubmed-meshheading:16109376-RNA Polymerase II,
pubmed-meshheading:16109376-Transcription, Genetic,
pubmed-meshheading:16109376-Transcription Factors
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pubmed:year |
2005
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pubmed:articleTitle |
The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription.
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pubmed:affiliation |
Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.
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pubmed:publicationType |
Journal Article
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