TY - JOUR
T1 - Human mediator subunit MED26 functions as a docking site for transcription elongation factors
AU - Takahashi, Hidehisa
AU - Parmely, Tari J.
AU - Sato, Shigeo
AU - Tomomori-Sato, Chieri
AU - Banks, Charles A.S.
AU - Kong, Stephanie E.
AU - Szutorisz, Henrietta
AU - Swanson, Selene K.
AU - Martin-Brown, Skylar
AU - Washburn, Michael P.
AU - Florens, Laurence
AU - Seidel, Chris W.
AU - Lin, Chengqi
AU - Smith, Edwin R.
AU - Shilatifard, Ali
AU - Conaway, Ronald C.
AU - Conaway, Joan W.
N1 - Funding Information:
We thank T. Suganuma for helpful discussions, M. Thirman for a generous gift of the anti-EAF1 antibody, K. Zueckert-Gaudenz and A. Peak for help with microarray experiments, and M. Katt and V. Neubauer for tissue culture. C.L. is a PhD thesis student registered with the Open University. This work was supported by funds from the Stowers Institute and by Grant GM41628 from NIGMS, NIH to J.W.C. and R.C.C.
PY - 2011/7/8
Y1 - 2011/7/8
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/79959939884
U2 - 10.1016/j.cell.2011.06.005
DO - 10.1016/j.cell.2011.06.005
M3 - Article
C2 - 21729782
AN - SCOPUS:79959939884
SN - 0092-8674
VL - 146
SP - 92
EP - 104
JO - Cell
JF - Cell
IS - 1
ER -