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Takahashi, Hidehisa; Parmely, Tari J.; Sato, Shigeo; Tomomori-Sato, Chieri; Banks, Charles A.S.; Kong, Stephanie E.; Szutorisz, Henrietta; Swanson, Selene K.; Martin-Brown, Skylar; Washburn, Michael P.; Florens, Laurence; Seidel, Chris W.; Lin, Chengqi; Smith, Edwin R.; Shilatifard, Ali; Conaway, Ronald C.; Conaway, Joan W.
Cell, 07/2011, Letnik: 146, Številka: 1Journal Article
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 super-elongation complexes (SECs) containing ELL/EAF family members, P-TEFb, and other proteins, but the mechanism of their recruitment is an 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. Display omitted ► Mediator subunit MED26 controls expression of genes regulated during elongation ► MED26 N-terminal domain (NTD) contributes to MED26-dependent gene regulation ► MED26 NTD recruits ELL- and P-TEFb-containing complexes to Mediator
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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Povezave do osebnih bibliografij avtorjev | Povezave do podatkov o raziskovalcih v sistemu SICRIS |
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Vir: Osebne bibliografije
in: SICRIS
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