Human mediator subunit MED26 functions as a docking site for transcription elongation factors.
Human mediator subunit MED26 functions as a docking site for transcription elongation factors.
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DOI:
10.1016/j.cell.2011.06.005
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发表时间:
2011-07-08
期刊:
影响因子:
64.5
通讯作者:
Conaway JW
中科院分区:
文献类型:
--
作者:
Takahashi H;Parmely TJ;Sato S;Tomomori-Sato C;Banks CA;Kong SE;Szutorisz H;Swanson SK;Martin-Brown S;Washburn MP;Florens L;Seidel CW;Lin C;Smith ER;Shilatifard A;Conaway RC;Conaway JW
Promoter proximal pausing by initiated RNA polymerase II (Pol II) and regulated release of paused polymerase into productive elongation has emerged as a major mechanism of transcription activation. Reactivation of paused Pol II correlates with recruitment of SuperElongationComplexes (SECs) containing ELL/EAF family members, P-TEFb, and other proteins, but the mechanism of their recruitment is currently a major unanswered question. Here, we present evidence for a role of human Mediator subunit Med26 in this process. We identify in the conserved N-terminal domain of Med26 overlapping docking sites for SEC and a second ELL/EAF-containing complex, as well as general initiation factor TFIID. In addition, we present evidence consistent with the model that Med26 can function as a molecular switch that interacts first with TFIID in the Pol II initiation complex and then exchanges TFIID for complexes containing ELL/EAF and P-TEFb to facilitate transition of Pol II into the elongation stage of transcription.
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通讯作者:
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