Human mediator subunit MED26 functions as a docking site for transcription elongation factors

Hidehisa Takahashi, Tari J. Parmely, Shigeo Sato, Chieri Tomomori-Sato, Charles A.S. Banks, Stephanie E. Kong, Henrietta Szutorisz, Selene K. Swanson, Skylar Martin-Brown, Michael P. Washburn, Laurence Florens, Chris W. Seidel, Chengqi Lin, Edwin R. Smith, Ali Shilatifard, Ronald C. Conaway, Joan W. Conaway

Research output: Contribution to journalArticlepeer-review

251 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)92-104
Number of pages13
Issue number1
StatePublished - Jul 8 2011
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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