TFIID component TAF7 functionally interacts with both TFIIH and P-TEFb

被引:32
作者
Gegonne, Anne [1 ]
Weissman, Jocelyn D. [1 ]
Lu, Hanxin [1 ]
Zhou, Meisheng [2 ]
Dasguptat, Arindam [2 ]
Ribble, Robert [2 ]
Brady, John N. [2 ]
Singer, Dinah S. [1 ]
机构
[1] NCI, Expt Immunol Branch, NIH, Bethesda, MD 20892 USA
[2] NCI, Tumor Virus Biol Lab, Basic Res Lab, NIH, Bethesda, MD 20892 USA
基金
美国国家卫生研究院;
关键词
MHC class I genes; regulation; transcription initiation;
D O I
10.1073/pnas.0801637105
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Transcription consists of a series of highly regulated steps: assembly of the preinitiation complex (PIC) at the promoter, initiation, elongation, and termination. PIC assembly is nucleated by TRID, a complex composed of the TATA-binding protein (TBP) and a series of TBP-associated factors (TAFs). One component, TAF7, is incorporated in the PIC through its interaction with TFIID but is released from TFIID upon transcription initiation. We now report that TAF7 interacts with the transcription factors, TFIIH and P-TEFb, resulting in the inhibition of their Pol II CTD kinase activities. Importantly, in in vitro transcription reactions, TAF7 inhibits steps after PIC assembly and formation of the first phosphodiester bonds. Further, in vivo TAF7 coelongates with P-TEFb and Pol II downstream of the promoter. We propose a model in which TAF7 contributes to the regulation of the transition from PIC. assembly to initiation and elongation.
引用
收藏
页码:5367 / 5372
页数:6
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