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

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.

Pubmed ID: 21729782


  • 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



Publication Data

July 8, 2011

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM41628
  • Agency: NIGMS NIH HHS, Id: R01 GM041628
  • Agency: NIGMS NIH HHS, Id: R01 GM041628-23

Mesh Terms

  • Cell Proliferation
  • Gene Expression Regulation
  • HSP70 Heat-Shock Proteins
  • HeLa Cells
  • Humans
  • Mediator Complex
  • Phosphorylation
  • Proto-Oncogene Proteins c-myc
  • RNA Polymerase II
  • Trans-Activators
  • Transcription, Genetic
  • Transcriptional Elongation Factors