File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4

TitleRecruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4
Authors
Issue Date2005
Citation
Molecular Cell, 2005, v. 19, n. 4, p. 535-545 How to Cite?
AbstractThe cyclinT1/Cdk9 heterodimer that constitutes core P-TEFb is generally presumed to be the transcriptionally active form for stimulating RNA polymerase II elongation. About half of cellular P-TEFb also exists in an inactive complex with the 7SK snRNA and the HEXIM1 protein. Here, we show that the remaining half associates with the bromodomain protein Brd4. In stress-induced cells, the 7SK/HEXIM1-bound P-TEFb is quantitatively converted into the Brd4-associated form. The association with Brd4 is necessary to form the transcriptionally active P-TEFb, recruits P-TEFb to a promoter, and enables P-TEFb to contact the Mediator complex, a potential target for the Brd4-mediated recruitment. Although generally required for transcription, the P-TEFb-recruitment function of Brd4 can be substituted by that of HIV-1 Tat, which recruits P-TEFb directly for activated HIV-1 transcription. Brd4, HEXIM1, and 7SK are all implicated in regulating cell growth, which may result from their dynamic control of the general transcription factor P-TEFb. Copyright ©2005 by Elsevier Inc.
Persistent Identifierhttp://hdl.handle.net/10722/323788
ISSN
2023 Impact Factor: 14.5
2023 SCImago Journal Rankings: 9.332
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYang, Zhiyuan-
dc.contributor.authorYik, Jasper H.N.-
dc.contributor.authorChen, Ruichuan-
dc.contributor.authorHe, Nanhai-
dc.contributor.authorMoon, Kyoo Jang-
dc.contributor.authorOzato, Keiko-
dc.contributor.authorZhou, Qiang-
dc.date.accessioned2023-01-13T02:59:20Z-
dc.date.available2023-01-13T02:59:20Z-
dc.date.issued2005-
dc.identifier.citationMolecular Cell, 2005, v. 19, n. 4, p. 535-545-
dc.identifier.issn1097-2765-
dc.identifier.urihttp://hdl.handle.net/10722/323788-
dc.description.abstractThe cyclinT1/Cdk9 heterodimer that constitutes core P-TEFb is generally presumed to be the transcriptionally active form for stimulating RNA polymerase II elongation. About half of cellular P-TEFb also exists in an inactive complex with the 7SK snRNA and the HEXIM1 protein. Here, we show that the remaining half associates with the bromodomain protein Brd4. In stress-induced cells, the 7SK/HEXIM1-bound P-TEFb is quantitatively converted into the Brd4-associated form. The association with Brd4 is necessary to form the transcriptionally active P-TEFb, recruits P-TEFb to a promoter, and enables P-TEFb to contact the Mediator complex, a potential target for the Brd4-mediated recruitment. Although generally required for transcription, the P-TEFb-recruitment function of Brd4 can be substituted by that of HIV-1 Tat, which recruits P-TEFb directly for activated HIV-1 transcription. Brd4, HEXIM1, and 7SK are all implicated in regulating cell growth, which may result from their dynamic control of the general transcription factor P-TEFb. Copyright ©2005 by Elsevier Inc.-
dc.languageeng-
dc.relation.ispartofMolecular Cell-
dc.titleRecruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.molcel.2005.06.029-
dc.identifier.pmid16109377-
dc.identifier.scopuseid_2-s2.0-23744467035-
dc.identifier.volume19-
dc.identifier.issue4-
dc.identifier.spage535-
dc.identifier.epage545-
dc.identifier.isiWOS:000231458000012-
dc.identifier.f10001027651-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats